B4U8B1 (B4U8B1_HYDS0) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Glutamyl-tRNA reductase HAMAP MF_00087
Short name=GluTR HAMAP MF_00087
EC=1.2.1.70 HAMAP MF_00087

Gene names

Name:	hemA HAMAP MF_00087
Ordered Locus Names:	HY04AAS1_0685

Organism

Hydrogenobaculum sp. (strain Y04AAS1) [Complete proteome] [HAMAP]

Taxonomic identifier

380749 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Hydrogenobaculum

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
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. HAMAP MF_00087
Catalytic activity	L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214
Subunit structure	Homodimer By similarity. HAMAP MF_00087
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. HAMAP MF_00087
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. HAMAP MF_00087
Sequence similarities	Belongs to the glutamyl-tRNA reductase family. HAMAP MF_00087 RuleBase RU000584

Ontologies

Keywords
Biological process	Porphyrin biosynthesis HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214
Ligand	NADP HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214
Molecular function	Oxidoreductase HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214 EMBL ACG57372.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	porphyrin-containing compound biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Nucleotide binding	188 – 193	6	NADP By similarity HAMAP MF_00087
	Region	51 – 54	4	Substrate binding By similarity HAMAP MF_00087
	Region	113 – 115	3	Substrate binding By similarity HAMAP MF_00087
Sites
	Active site	52	1	Nucleophile By similarity HAMAP MF_00087
	Binding site	108	1	Substrate By similarity HAMAP MF_00087
	Binding site	119	1	Substrate By similarity HAMAP MF_00087
	Site	98	1	Important for activity By similarity HAMAP MF_00087

Sequences

	Sequence		Length	Mass (Da)
	B4U8B1 [UniParc]. Last modified September 23, 2008. Version 1. Checksum: 26E79A01B05E9178	FASTA	398	45,046
	10 20 30 40 50 60 MAGDIYAVGL NYKTAAVELR EKLSCDTSEL DSILHILKAS TNVKEFMLLS TCNRLELYAY 70 80 90 100 110 120 ASNEKFVLDA FRRYAEIKNQ SVDNSHLFLK AGKEAVAHIF KVASGLDSMV IGEPQIVAQF 130 140 150 160 170 180 KEAFFKAKAS GTTGKVMNRL CQNALHASKR VRYETGISKS AVSVSYAAVE LAKRIFGELK 190 200 210 220 230 240 NHKVLLIGAG EMGELAAIYL QRSGASIYIS NRTYERAVSL AEKIKANVIR FDEIEQFLYE 250 260 270 280 290 300 FDVVLVSTGA QGYVITKDVV SKAMKKRYYK PIFLIDISVP RNIEPSCADL DSVFLYNVDD 310 320 330 340 350 360 LKEVVENNLS NRIQEAKKGE FIILDEADKF YKWLENLELE PIIINMLDYT KNGSKDCKKI 370 380 390 VYRAIKLIRE NKEYTPLVFE LLGIKFKAKE IDYGFVER

References

[1]

"Complete and draft genome sequences of six members of the Aquificales." Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A. J. Bacteriol. 191:1992-1993(2009) [PubMed: 19136599] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001130 Genomic DNA. Translation: ACG57372.1.
RefSeq	YP_002121350.1. NC_011126.1.
3D structure databases
ProteinModelPortal	B4U8B1.
ModBase	Search...
Protein-protein interaction databases
STRING	B4U8B1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6743487.
GenomeReviews	Gene locus HY04AAS1_0685 in contig CP001130_GR.
KEGG	hya:HY04AAS1_0685.
PATRIC	22136032. VBIHydSp64203_0688.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG732626.
OMA	PESSHAT.
ProtClustDB	PRK00045.
Family and domain databases
HAMAP	MF_00087. Glu_tRNA_reductase. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR016040. NAD(P)-bd_dom. IPR018214. Pyrrol_synth_GluRdtase_CS. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K02492.
Pfam	PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit. [Graphical view]
PIRSF	PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAM	SSF69742. GlutR. 1 hit.
TIGRFAMs	TIGR01035. HemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

B4U8B1_HYDS0

Accession

Primary (citable) accession number: B4U8B1

Entry history

Integrated into UniProtKB/TrEMBL:	September 23, 2008
Last sequence update:	September 23, 2008
Last modified:	December 14, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)