NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VF5;
DOI=10.1038/32831; PubMed=9537320 [NCBI, ExPASy, EBI, Israel, Japan]
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
Nature 392:353-358(1998).

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

AE000657; AAC07274.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

G70410; G70410.

RefSeq

NP_213878.1; -.

3D structure databases

HSSP

Q9UXR8; 1GPJ. [HSSP ENTRY / PDB]

ModBase

O67314.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_1279-MON; -.

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.
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

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

1192752; -.

GenomeReviews

AE000657_GR; aq_1279.

KEGG

aae:aq_1279; -.

NMPDR

fig|224324.1.peg.893; -.

Phylogenomic databases

HOGENOM

O67314; -.

Genome annotation databases

CMR

O67314; aq_1279.

Other

ProtoNet

O67314.

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`	`1 406`	`406`	`Glutamyl-tRNA reductase.`	`PRO_0000113987`
`NP_BIND`	`187 192`	`6`	`NADP (By similarity).`
`REGION`	`50 53`	`4`	`Substrate binding (By similarity).`
`REGION`	`112 114`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`51 51`		`Nucleophile (By similarity).`
`BINDING`	`107 107`		`Substrate (By similarity).`
`BINDING`	`118 118`		`Substrate (By similarity).`
`SITE`	`97 97`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 406 AA [This is the length of the unprocessed precursor]

Molecular weight: 46648 Da [This is the MW of the unprocessed precursor]

CRC64: 77F3ECC488FC4394 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGEIFVAGVN FKVAPVEVRE KLACSLEETK KVLPILKRET PLEEVMLLST CNRVEVYAYN 

        70         80         90        100        110        120 
FVENSEDLIN KLLEIKRLNP SFKRYFFVKR GEEAVYHIFK VASSLDSMVI GEPQIVAQFK 

       130        140        150        160        170        180 
EAYRVAKEAG TVGKILNRVY EKALRASKRV RTETGISRSA VSVSYAAVEL AKKIFGDLKE 

       190        200        210        220        230        240 
AKVLLIGAGE MGELAANYLR RFGAKLHITN RTYERALKLV KELSGNVLRF EELKEYLPLM 

       250        260        270        280        290        300 
DIVIVSTGAK DYILKREDFE RSVRERHYEP QFVIDIAVPR NVDPEAGNVE GVFLYDIDDL 

       310        320        330        340        350        360 
KQVVEENLKE RIKEAQRGEI ILWDEVKKFM NWYESLKAEP YILELKASVE GKEVSPYIKK 

       370        380        390        400 
LVHRAIKEIK RNPEVADIIL RIFKEVEKNE PRRKELSNVY NGTHGA

O67314 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