NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Woelfle M.A., Haselkorn R.;
"Cloning and characterization of hemA, a gene encoding glutamyl tRNA reductase in the cyanobacterium Anabaena sp. strain 7120.";
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1093/dnares/8.5.205; PubMed=11759840 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M., Yasuda M., Tabata S.;
"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120.";
DNA Res. 8:205-213(2001).

Comments

FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) (By similarity).
CATALYTIC ACTIVITY: L-glutamate 1-semialdehyde + NADP⁺ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.
PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2 .
PATHWAY: Porphyrin biosynthesis; chlorophyll biosynthesis .
SUBUNIT: Homodimer (By similarity).
DOMAIN: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization (By similarity).
MISCELLANEOUS: During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA (By similarity).
SIMILARITY: Belongs to the glutamyl-tRNA reductase family.

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

U97695; AAB58164.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000019; BAB72999.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

AG1936; AG1936.

RefSeq

NP_485085.1; -.

3D structure databases

HSSP

Q9UXR8; 1GPJ. [HSSP ENTRY / PDB]

ModBase

O08393.

Enzyme and pathway databases

BioCyc

NSP103690:ALR1042-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0008883;	Molecular function: glutamyl-tRNA reductase activity (inferred from electronic annotation from HAMAP).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0004764;	Molecular function: shikimate 5-dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0015995;	Biological process: chlorophyll biosynthetic 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

HAMAP

MF_00087; -; 1.
PBIL [Tree]

InterPro

IPR000343; 4pyrrol_synth_GluRdtase.
IPR015896; 4pyrrol_synth_GluRdtase_C.
IPR015895; 4pyrrol_synth_GluRdtase_N.
IPR016040; NAD(P)-bd.
IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF00745; GlutR_dimer; 1.
PF05201; GlutR_N; 1.
PF01488; Shikimate_DH; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000445; 4pyrrol_synth_GluRdtase; 1.

TIGRFAMs

TIGR01035; hemA; 1.

PROSITE

PS00747; GLUTR; 1.

Genome annotation databases

GeneID

1104636; -.

GenomeReviews

BA000019_GR; alr1042.

KEGG

ana:alr1042; -.

NMPDR

fig|103690.1.peg.1352; -.

Phylogenomic databases

HOGENOM

O08393; -.

Genome annotation databases

CMR

O08393; alr1042.

Other

ProtoNet

O08393.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Chlorophyll biosynthesis; Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 428`	`428`	`Glutamyl-tRNA reductase.`	`PRO_0000113986`
`NP_BIND`	`189 194`	`6`	`NADP (By similarity).`
`REGION`	`49 52`	`4`	`Substrate binding (By similarity).`
`REGION`	`114 116`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`50 50`		`Nucleophile (By similarity).`
`BINDING`	`109 109`		`Substrate (By similarity).`
`BINDING`	`120 120`		`Substrate (By similarity).`
`SITE`	`99 99`	`1`	`Important for activity (By similarity).`
`CONFLICT`	`33 33`		`A -> G (in Ref. 1; AAB58164).`
`CONFLICT`	`48 48`		`S -> G (in Ref. 1; AAB58164).`
`CONFLICT`	`174 174`		`Q -> E (in Ref. 1; AAB58164).`
`CONFLICT`	`280 280`		`I -> V (in Ref. 1; AAB58164).`
`CONFLICT`	`374 380`		`DKHQEVI -> EQTSRGV (in Ref. 1; AAB58164).`

Sequence information

Length: 428 AA [This is the length of the unprocessed precursor]

Molecular weight: 47909 Da [This is the MW of the unprocessed precursor]

CRC64: 06A470955F9D3C64 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNIAVVGLSH KTAPVEIREK LSIPEPQTES AIAQLTSYPH IDEVAILSTC NRLEIYIVAG 

        70         80         90        100        110        120 
ETDHGIREVT QFLSEHSKLP VHSLRQHLFV LLHEDAVMHI MRVAAGLDSL VLGEGQILAQ 

       130        140        150        160        170        180 
VKNTHKLGQQ YNGIKTILNR LFKQALTAGK RVRTETSIGT GAVSISSAAV ELAQIKAENL 

       190        200        210        220        230        240 
AACRVTILGA GKMSRLLVQH LVSKGATQIS IVNRSRERAQ ELAKQFSEHP IRTHLLPEMM 

       250        260        270        280        290        300 
TVIAESHLVF TSTSATEPIL DRAKLEMVLA PNQPLMLFDI SVPRNVHTDV NELVNVQAFN 

       310        320        330        340        350        360 
VDDLKAVVAQ NYESRRKMAQ EAERLLEEEI EAFDIWWRSL ETVSTISSLR SKIETIREQE 

       370        380        390        400        410        420 
LEKALSRLGS EFGDKHQEVI EALTRGIVNK ILHDPMVQLR AQQDVEARRR CMQTLQMLFN 


LDVGEQFS

O08393 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools