ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P09831


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name GLTB_ECOLI
Primary accession number P09831
Secondary accession number Q2M900
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on November 1, 1995 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 90)
Name and origin of the protein
Protein name Glutamate synthase [NADPH] large chain [Precursor]
Synonyms EC 1.4.1.13
Glutamate synthase subunit alpha
GLTS alpha chain
NADPH-GOGAT
Gene name
Name: gltB
Synonyms: aspB
OrderedLocusNames: b3212, JW3179
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=K12;
DOI=10.1016/0378-1119(87)90207-1; PubMed=3326786 [NCBI, ExPASy, EBI, Israel, Japan]
Oliver G., Gosset G., Sanchez-Pescador R., Lozoya E., Ku L.M., Flores N., Becerril B., Valle F., Bolivar F.;
"Determination of the nucleotide sequence for the glutamate synthase structural genes of Escherichia coli K-12.";
Gene 60:1-11(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-304.
PubMed=1673677 [NCBI, ExPASy, EBI, Israel, Japan]
Velazquez L., Camarena L., Reyes J.L., Bastarrachea F.;
"Mutations affecting the Shine-Dalgarno sequences of the untranslated region of the Escherichia coli gltBDF operon.";
J. Bacteriol. 173:3261-3264(1991).
[5]
DISCUSSION OF SEQUENCE.
PubMed=2643092 [NCBI, ExPASy, EBI, Israel, Japan]
Gosset G., Merino E., Recillas F., Oliver G., Becerril B., Bolivar F.;
"Amino acid sequence analysis of the glutamate synthase enzyme from Escherichia coli K-12.";
Protein Seq. Data Anal. 2:9-16(1989).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M18747; AAA23904.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U18997; AAA58014.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76244.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77256.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68876; AAA23906.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR F65112; F65112.
RefSeq AP_003755.1; -.
NP_417679.1; -.
3D structure databases
HSSP P55038; 1LM1. [HSSP ENTRY / PDB]
ModBase P09831.
Protein-protein interaction databases
DIP DIP:9802N; -.
IntAct P09831; 8.
Enzyme and pathway databases
BioCyc EcoCyc:GLUSYNLARGE-MON; -.
MetaCyc:GLUSYNLARGE-MON; -.
Organism-specific databases
EchoBASE EB0398; -.
EcoGene EG10403; gltB.
Ontologies
GO
GO:0051538; Molecular function: 3 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004355; Molecular function: glutamate synthase (NADPH) activity (inferred from electronic annotation from EC).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006537; Biological process: glutamate biosynthetic process (inferred from electronic annotation from InterPro).
GO:0006541; Biological process: glutamine metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013785; Aldolase_TIM.
IPR000583; GATase_2.
IPR002932; Glu_synth_centr_C.
IPR006982; Glu_synth_centr_N.
IPR002489; Glu_synthase_C.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 2.
G3DSA:2.160.20.60; Glu_synthase_C; 1.
Pfam PF00310; GATase_2; 1.
PF04898; Glu_syn_central; 1.
PF01645; Glu_synthase; 1.
PF01493; GXGXG; 1.
Pfam graphical view of domain structure.
PROSITE PS51278; GATASE_TYPE_2; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 947724; -.
GenomeReviews AP009048_GR; JW3179.
U00096_GR; b3212.
KEGG ecj:JW3179; -.
eco:b3212; -.
Phylogenomic databases
HOGENOM P09831; -.
Other
LinkHub P09831; -.
Genome annotation databases
CMR P09831; b3212.
Other
ProtoNet P09831.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3Fe-4S; Amino-acid biosynthesis; Complete proteome; Direct protein sequencing; FAD; Flavoprotein; FMN; Glutamate biosynthesis; Glutamine amidotransferase; Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
PROPEP   1     42  42      PRO_0000011620
CHAIN   43   1517  1475     Glutamate synthase [NADPH] large chain. PRO_0000011621
DOMAIN   43    433  391     Glutamine amidotransferase type-2. 
NP_BIND   1080   1132  53     FMN (By similarity). 
ACT_SITE   43     43        For GATase activity (By similarity). 
METAL   1133   1133        Iron-sulfur (3Fe-4S) (By similarity). 
METAL   1139   1139        Iron-sulfur (3Fe-4S) (By similarity). 
METAL   1144   1144        Iron-sulfur (3Fe-4S) (By similarity). 
CONFLICT   105    109        GWRLA -> LAFR (in Ref. 1; AAA23904). 
CONFLICT   140    140        E -> N (in Ref. 1; AAA23904). 
CONFLICT   220    240        LCMPTDLPRFYLDLADLRLES -> CVCRRICRVLSGSCGPASGM (in Ref. 1; AAA23904). 
CONFLICT   259    282        LAQPFRYLAHNGEINTITGNRQWA -> WRNRSAIWRITVKSTPSPVTANG (in Ref. 1 and 4). 
CONFLICT   460    460        N -> K (in Ref. 1; AAA23904). 
CONFLICT   574    574        A -> T (in Ref. 1; AAA23904). 
CONFLICT   863    863        D -> H (in Ref. 1; AAA23904). 
CONFLICT   1286   1290        THGDQ -> DARRS (in Ref. 1; AAA23904). 
CONFLICT   1373   1373        G -> A (in Ref. 1; AAA23904). 
CONFLICT   1376   1376        G -> R (in Ref. 1; AAA23904). 
Sequence information
Length: 1517 AA [This is the length of the unprocessed precursor] Molecular weight: 166710 Da [This is the MW of the unprocessed precursor] CRC64: 7524A143B5DD4F9A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTRKPRRHAL SVPVRSGSEV GFPQSLGEVH DMLYDKSLER DNCGFGLIAH IEGEPSHKVV 

        70         80         90        100        110        120 
RTAIHALARM QHRGAILADG KTGDGCGLLL QKPDRFFRIV AQERGWRLAK NYAVGMLFLN 

       130        140        150        160        170        180 
KDPELAAAAR RIVEEELQRE TLSIVGWRDV PTNEGVLGEI ALSSLPRIEQ IFVNAPAGWR 

       190        200        210        220        230        240 
PRDMERRLFI ARRRIEKRLE ADKDFYVCSL SNLVNIYKGL CMPTDLPRFY LDLADLRLES 

       250        260        270        280        290        300 
AICLFHQRFS TNTVPRWPLA QPFRYLAHNG EINTITGNRQ WARARTYKFQ TPLIPDLHDA 

       310        320        330        340        350        360 
APFVNETGSD SSSMDNMLEL LLAGGMDIIR AMRLLVPPAW QNNPDMDPEL RAFFDFNSMH 

       370        380        390        400        410        420 
MEPWDGPAGI VMSDGRFAAC NLDRNGLRPA RYVITKDKLI TCASEVGIWD YQPDEVVEKG 

       430        440        450        460        470        480 
RVGPGELMVI DTRSGRILHS AETDDDLKSR HPYKEWMEKN VRRLVPFEDL PDEEVGSREL 

       490        500        510        520        530        540 
DDDTLASYQK QFNYSAEELD SVIRVLGENG QEAVGSMGDD TPFAVLSSQP RIIYDYFRQQ 

       550        560        570        580        590        600 
FAQVTNPPID PLREAHVMSL ATSIGREMNV FCEAEGQAHR LSFKSPILLY SDFKQLTTMK 

       610        620        630        640        650        660 
EEHYRADTLD ITFDVTKTTL EATVKELCDK AEKMVRSGTV LLVLSDRNIA KDRLPVPAPM 

       670        680        690        700        710        720 
AVGAIQTRLV DQSLRCDANI IVETASARDP HHFAVLLGFG ATAIYPYLAY ETLGRLVDTH 

       730        740        750        760        770        780 
AIAKDYRTVM LNYRNGINKG LYKIMSKMGI STIASYRCSK LFEAVGLHDD VVGLCFQGAV 

       790        800        810        820        830        840 
SRIGGASFED FQQDLLNLSK RAWLARKPIS QGGLLKYVHG GEYHAYNPDV VRTLQQAVQS 

       850        860        870        880        890        900 
GEYSDYQEYA KLVNERPATT LRDLLAITPG ENAVNIADVE PASELFKRFD TAAMSIGALS 

       910        920        930        940        950        960 
PEAHEALAEA MNSIGGNSNS GEGGEDPARY GTNKVSRIKQ VASGRFGVTP AYLVNADVIQ 

       970        980        990       1000       1010       1020 
IKVAQGAKPG EGGQLPGDKV TPYIAKLRYS VPGVTLISPP PHHDIYSIED LAQLIFDLKQ 

      1030       1040       1050       1060       1070       1080 
VNPKAMISVK LVSEPGVGTI ATGVAKAYAD LITIAGYDGG TGASPLSSVK YAGCPWELGL 

      1090       1100       1110       1120       1130       1140 
VETQQALVAN GLRHKIRLQV DGGLKTGVDI IKAAILGAES FGFGTGPMVA LGCKYLRICH 

      1150       1160       1170       1180       1190       1200 
LNNCATGVAT QDDKLRKNHY HGLPFKVTNY FEFIARETRE LMAQLGVTRL VDLIGRTDLL 

      1210       1220       1230       1240       1250       1260 
KELDGFTAKQ QKLALSKLLE TAEPHPGKAL YCTENNPPFD NGLLNAQLLQ QAKPFVDERQ 

      1270       1280       1290       1300       1310       1320 
SKTFWFDIRN TDRSVGASLS GYIAQTHGDQ GLAADPIKAY FNGTAGQSFG VWNAGGVELY 

      1330       1340       1350       1360       1370       1380 
LTGDANDYVG KGMAGGLIAI RPPVGSAFRS HEASIIGNTC LYGATGGRLY AAGRAGERFG 

      1390       1400       1410       1420       1430       1440 
VRNSGAITVV EGIGDNGCEY MTGGIVCILG KTGVNFGAGM TGGFAYVLDE SGDFRKRVNP 

      1450       1460       1470       1480       1490       1500 
ELVEVLSVDA LAIHEEHLRG LITEHVQHTG SQRGEEILAN WSTFATKFAL VKPKSSDVKA 

      1510 
LLGHRSRSAA ELRVQAQ 

P09831 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!