NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P.;
"Complete sequence of Actinobacillus succinogenes 130Z.";
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.

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 .
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

CP000746; ABR74482.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001344417.1; -.

3D structure databases

ModBase

A6VND5.

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

5348066; -.

GenomeReviews

CP000746_GR; Asuc_1116.

CMR

A6VND5; Asuc_1116.

Other

ProtoNet

A6VND5.

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`	`1 435`	`435`	`Glutamyl-tRNA reductase.`	`PRO_1000071245`
`NP_BIND`	`204 209`	`6`	`NADP (By similarity).`
`REGION`	`49 52`	`4`	`Substrate binding (By similarity).`
`REGION`	`119 121`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`50 50`		`Nucleophile (By similarity).`
`BINDING`	`114 114`		`Substrate (By similarity).`
`BINDING`	`125 125`		`Substrate (By similarity).`
`SITE`	`104 104`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 435 AA [This is the length of the unprocessed precursor]

Molecular weight: 49073 Da [This is the MW of the unprocessed precursor]

CRC64: F6A876382802D60B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTILVLGINH KTATVALREK VAFSEEKRLS ALNQIEQLKL AQSTVILSTC NRTEVYLHNK 

        70         80         90        100        110        120 
FIQPEQNSAW IDECVAWFAA IHQIQLTDLQ DCLYFYQNQQ AVTHLMRVAC GLDSLILGEP 

       130        140        150        160        170        180 
QILGQVKQAY QLAEEYYQRA HGLGKSAVIS SELSRLFQKT FSTAKRVRTE TNIGESAVSV 

       190        200        210        220        230        240 
AYAACSLGRQ IFESLQELTI LLVGAGETIE LAARHLLRHG VKKLMIANRT RARAEALVAK 

       250        260        270        280        290        300 
LESPFIEILS LSELQDGLNQ ADIVISSTGS PTTLISYEMM KQAQIQRRYR PVLIVDIAVP 

       310        320        330        340        350        360 
RDVEESIVKL DSVYHYTVDD LQNIINHNLS EREKASEQAE EIIAEECAAF FEWLKVRQAS 

       370        380        390        400        410        420 
NLIRTYRESA DEIRQELLEK AQFSLSQGES ADKILDEFST KLMNKLLHSP TLVMQTMVKQ 

       430 
GDSRGLQNFL SVIKK

A6VND5 in FASTA format

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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