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UniProtKB/Swiss-Prot entry A4XJN9

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

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Entry information
Entry name ARGC_CALS8
Primary accession number A4XJN9
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on May 29, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 15)
Name and origin of the protein
Protein name N-acetyl-gamma-glutamyl-phosphate reductase
Synonyms AGPR
EC 1.2.1.38
N-acetyl-glutamate semialdehyde dehydrogenase
NAGSA dehydrogenase
Gene name
Name: argC
OrderedLocusNames: Csac_1531
From
Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [TaxID: 351627] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P.;
"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903.";
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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
CP000679; ABP67124.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001180315.1; -.
3D structure databases
ModBase A4XJN9.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003942; Molecular function: N-acetyl-gamma-glutamyl-phosphate reductase activity (inferred from electronic annotation from HAMAP).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0046983; Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0006526; Biological process: arginine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_00150; -; 1.
PBIL [Tree]
InterPro IPR000706; AGPR_act_site.
IPR016040; NAD(P)-bd.
IPR000534; Semialdehyde_DHase_NAD-bd.
IPR012280; Semialdhyde_DHase_C.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF01118; Semialdhyde_dh; 1.
PF02774; Semialdhyde_dhC; 1.
Pfam graphical view of domain structure.
ProDom PD003765; AGPR_act_site; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01850; argC; 1.
PROSITE PS01224; ARGC; 1.
Genome annotation databases
GeneID 5088113; -.
GenomeReviews CP000679_GR; Csac_1531.
KEGG csc:Csac_1531; -.
CMR A4XJN9; Csac_1531.
Other
ProtoNet A4XJN9.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; Cytoplasm; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   343  343     N-acetyl-gamma-glutamyl-phosphate reductase. PRO_1000010983
ACT_SITE   148   148        By similarity. 
Sequence information
Length: 343 AA [This is the length of the unprocessed precursor] Molecular weight: 38574 Da [This is the MW of the unprocessed precursor] CRC64: 1AA8E0A4DE8975F5 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIKASIIGAS GYVGIELIRL LLKHPEVEIS SIISSSNKDI SIENTNPQFK KILNLTFKEF 

        70         80         90        100        110        120 
DIDLVKEADV VFCALPHGVS QEYVKVAYDL GKVVIDLSSD FRYKDLTRYS KDYGNHKYPE 

       130        140        150        160        170        180 
LLNESSYGLC EIFREEIKSS KIVGNPGCYP TSAILGLAPL LKNKLIQKDS IIIDSKSGVS 

       190        200        210        220        230        240 
GAGKKADFAY SFCEVDENFK AYGVAKHRHT SEIEEKCSFL FGEDLNLSFT PHLLPVKRGI 

       250        260        270        280        290        300 
LSTIYATFTK SLNKNELIEI YKEFYRDEFF IRIYEDSLPE LKYVTGTNFV DIGLEVDKKT 

       310        320        330        340 
NRVIVISCID NLIKGAAGQA IQNMNIKFSL NEKTGLVIVG EYF
A4XJN9 in FASTA format

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