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 .
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

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Cross-references

Sequence databases

EMBL

CP000885; ABX41743.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001558482.1; -.

3D structure databases

ModBase

A9KP81.

Ontologies

GO:0008883;	Molecular function: glutamyl-tRNA reductase activity (inferred from electronic annotation from HAMAP).
GO:0006779;	Biological process: porphyrin biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00087; -; 1.
PBIL [Tree]

InterPro

IPR000343; 4pyrrol_synth_GluRdtase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

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

TIGRFAMs

TIGR01035; hemA; 1.

PROSITE

PS00747; GLUTR; FALSE_NEG.

BLOCKS

A9KP81.

Genome annotation databases

GeneID

5742318; -.

GenomeReviews

CP000885_GR; Cphy_1368.

KEGG

cpy:Cphy_1368; -.

CMR

A9KP81; Cphy_1368.

Other

ProtoNet

A9KP81.

UniRef

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

Keywords

Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 403`	`403`	`Glutamyl-tRNA reductase 1.`	`PRO_0000335023`
`NP_BIND`	`183 188`	`6`	`NADP (By similarity).`
`REGION`	`45 48`	`4`	`Substrate binding (By similarity).`
`REGION`	`108 110`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`46 46`		`Nucleophile (By similarity).`
`BINDING`	`103 103`		`Substrate (By similarity).`
`BINDING`	`114 114`		`Substrate (By similarity).`
`SITE`	`93 93`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 403 AA [This is the length of the unprocessed precursor]

Molecular weight: 46029 Da [This is the MW of the unprocessed precursor]

CRC64: 497F1715C4F6418F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLGIDHNKAS IEEREIFSFT KKMAADVLLN IKEIEGINGC IILSTCNRME VWVSCFEEFE 

        70         80         90        100        110        120 
TSIYEILCSI KKVDDNRYRH CFIERGGYDA IEHLFYMTCG LKSKIIGEDQ ILTQVREALE 

       130        140        150        160        170        180 
LSRENYCTDS VLETLFRFAI TSAKQVKTQI HLSVVNSSVI HHVVHELKLS NYLFKGKKCL 

       190        200        210        220        230        240 
VIGNGEMGKL AATKLEEEGS DVTVTVRQYR SGIIEIPVGC NRINYGDRLE HIVEYDFVIS 

       250        260        270        280        290        300 
ATSSPNMTIH LEQLSNLEFK KPVLFIDLAV PRDIDPRITE LKNITLYDID HFKVETVSDE 

       310        320        330        340        350        360 
MKTQLRQIDE ILKTKMDEFI SWYECRGIIK VVQTLSENAA IDVGLRIDKT MKKIEMDSND 

       370        380        390        400 
KELLAATVHS ATNKVVSKLM FGLRDHVSAA TFQECMVALK NIY

A9KP81 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