Reviewed, UniProtKB/Swiss-Prot Q0VS78 (HEM1_ALCBS)

Names and origin

Protein names

Recommended name:
    Glutamyl-tRNA reductase
      Short name=GluTR
    EC=1.2.1.70

Gene names

Name:	hemA
Ordered Locus Names:	ABO_0522

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	418 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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 structure	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.
Sequence similarities	Belongs to the glutamyl-tRNA reductase family.

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW porphyrin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: HAMAP shikimate 5-dehydrogenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 418	418	Glutamyl-tRNA reductase		PRO_1000004590
Regions
	Nucleotide binding	186 – 191	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	111 – 113	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	106	1	Substrate By similarity
	Binding site	117	1	Substrate By similarity
	Site	96	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0VS78-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 09415E69BADCE528	FASTA	418	46,630
	10 20 30 40 50 60 MNLVAVGVNH TTADVELRER LAFSTQQAEV ALASLREMPG VREAALLSTC NRTELYCLTD 70 80 90 100 110 120 DVTPNFAQWL ASSRNLSVER LSTVLYQHTG EQALEHMMRV AGGLDSLVLG EPQILGQMRE 130 140 150 160 170 180 AYARAHEAGL LNGELSRLFQ EVFSVAKRIR TETGIGANPV SVAYAAVSFA RHIFADLKKS 190 200 210 220 230 240 RALLIGAGEM IELVARHLSE QQVQEITIAN RTQERASELA AAVGGRGISL EELPVALERA 250 260 270 280 290 300 DILISCTAAP LPIMGKGMVE RALKKRRHRP MFMVDIAVPR DIEPEVGELG DVYLYTVDHL 310 320 330 340 350 360 QEAIQENVRS RQQAAQEASE LIRDAIVRHR RQRREQDAVK VLRDYREQRK AMAESELEKA 370 380 390 400 410 LQQLRNGGDA EQVLRRFQHS LVNKWLHSPS VTLRKMAADG RAEALLLARE LLLDDDQS

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM286690 Genomic DNA. Translation: CAL15970.1.
RefSeq	YP_692242.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4212665.
GenomeReviews	Gene locus ABO_0522 in contig AM286690_GR.
KEGG	abo:ABO_0522.
NMPDR	fig|393595.12.peg.518.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0VS78.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_0522-MON.
Family and domain databases
HAMAP	MF_00087. [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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00745. GlutR_dimer. 1 hit. PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit. [Graphical view]
PIRSF	PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
TIGRFAMs	TIGR01035. hemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_ALCBS

Accession

Primary (citable) accession number: Q0VS78

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	November 25, 2008
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)