NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1101/gad.1510307; PubMed=17344419 [NCBI, ExPASy, EBI, Israel, Japan]
Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M.;
"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis.";
Genes Dev. 21:601-614(2007).

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

CP000521; ABO11271.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001083873.1; -.

3D structure databases

ModBase

A3M2X7.

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.

TIGR01035; hemA; 1.

PS00747; GLUTR; 1.

Genome annotation databases

GeneID

4917062; -.

GenomeReviews

CP000521_GR; A1S_0837.

KEGG

acb:A1S_0837; -.

NMPDR

fig|400667.4.peg.861; -.

CMR

A3M2X7; A1S_0837.

Other

ProtoNet

A3M2X7.

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`	`1 427`	`427`	`Glutamyl-tRNA reductase.`	`PRO_0000335003`
`NP_BIND`	`185 190`	`6`	`NADP (By similarity).`
`REGION`	`49 52`	`4`	`Substrate binding (By similarity).`
`REGION`	`110 112`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`50 50`		`Nucleophile (By similarity).`
`BINDING`	`105 105`		`Substrate (By similarity).`
`BINDING`	`116 116`		`Substrate (By similarity).`
`SITE`	`95 95`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 427 AA [This is the length of the unprocessed precursor]

Molecular weight: 47964 Da [This is the MW of the unprocessed precursor]

CRC64: A42E068563D88393 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSFFALGVNH QTASVELREQ IAFNAERLSN LLAEQRHHES LKDLVVVSTC NRTEVYAMAE 

        70         80         90        100        110        120 
DAESLLKWLA DANNIDVKQL IHHVYRYENA QAITHLMRVA SGLDSLMLGE PQILGQVKSA 

       130        140        150        160        170        180 
LALSKEAQTV SPELNSVFEY AFYAAKRVRS ETAVGSHAVS MGYAVAQLAL QVFSKPEKLT 

       190        200        210        220        230        240 
VMVVAAGEMN SLVAKHLAEM GVAKMIICNR SRERADQLAQ EIAHQVEVEI IDFSDLAENL 

       250        260        270        280        290        300 
YRADVVSSCT GSLHQVIAYA DVKTALKKRR YQQMLMVDLA VPRDIDPKVE SLDGVYLYGV 

       310        320        330        340        350        360 
DDLQSVIDEN LAQRRQAAVE AEVMVNQLAT QLITHQKVKE AGSTIHAYRQ HSEEISQREL 

       370        380        390        400        410        420 
THALEALHHG GNPEQVLQQF AHRLTQKLIH PTSMLLREAA KAESPDYFEW LQQHLQDVFD 


HERKPKR

A3M2X7 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