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

CP000481; ABK52012.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_871998.1; -.

3D structure databases

ModBase

A0LRF2.

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.
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.

TIGR01035; hemA; 1.

PS00747; GLUTR; 1.

Genome annotation databases

GeneID

4485376; -.

GenomeReviews

CP000481_GR; Acel_0238.

KEGG

ace:Acel_0238; -.

CMR

A0LRF2; Acel_0238.

Other

ProtoNet

A0LRF2.

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`	`1 473`	`473`	`Glutamyl-tRNA reductase.`	`PRO_0000335000`
`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).`

Sequence information

Length: 473 AA [This is the length of the unprocessed precursor]

Molecular weight: 50720 Da [This is the MW of the unprocessed precursor]

CRC64: BBBB567B837D1ABF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLLVVGVSH RGTPLSLLER AVLDSDQATK LLDDLVGSPV VREGMVLSTC NRVEIYACVE 

        70         80         90        100        110        120 
KFHPALTLIS ELLSRHGNVN FDEIAGHVHV HYDDRAVQHL FAVAAGLDSM LIGEHQVVGQ 

       130        140        150        160        170        180 
VRDAFRLAQE RGYAGRDLHA IVQDALHAAR RVRAETRIDS AGQTLVDVGL QILSERLGPL 

       190        200        210        220        230        240 
AGRRALVIGA GAMASVAVAA LTRVGITGLT VASRTLRRAT ALAQRYNGQA AALEKLADLL 

       250        260        270        280        290        300 
AETDVVVSCT GSVHPVVDAA TLTKAVAGRT NPLGILDIAL PHDVDPDVDR LPNVIRVDLE 

       310        320        330        340        350        360 
TLRPVLENTA SSADVRHARH ILDEEFDAHV ARRAAVGVVP TVVALRDKAA RVVAAELRRL 

       370        380        390        400        410        420 
EKRLPELDPR QFEEIRTTVH RVVDKLLHAP TVRVQELAGL AGPDSYSEAL RTLFDLDPAQ 

       430        440        450        460        470 
PVAISAPQPS TDSPARAAYQ PTDEAATDAE PRRDDAEPPS AAAAQDAGRE SRP

A0LRF2 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 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