A0M6C1 (HEM1_GRAFK) Reviewed, UniProtKB/Swiss-Prot

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:	GFO_3223

Organism

Gramella forsetii (strain KT0803) [Complete proteome] [HAMAP]

Taxonomic identifier

411154 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Gramella

Protein attributes

Sequence length	418 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
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP MF_00087
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.

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	porphyrin-containing compound biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: EC
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 HAMAP MF_00087		PRO_0000335042
Regions
	Nucleotide binding	193 – 198	6	NADP By similarity
	Region	57 – 60	4	Substrate binding By similarity
	Region	118 – 120	3	Substrate binding By similarity
Sites
	Active site	58	1	Nucleophile By similarity
	Binding site	113	1	Substrate By similarity
	Binding site	124	1	Substrate By similarity
	Site	103	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0M6C1 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: 6CBDC8FB775EA398	FASTA	418	47,931
	10 20 30 40 50 60 MEDYHISRGK HFYTIGLSYK KADAEIRGHF SLTEESKQRL LEQAKEEGID GILVTSTCNR 70 80 90 100 110 120 TEIYGFAQHP FQLIKLLCEH THGTVEEFEK VAYVYKNKQA ITHIFKVGTG LDSQILGDFE 130 140 150 160 170 180 IISQLKIAFV RSKKLGLVNA FLERLVNAVI QASKRIKNET EISTGATSVS FASVQYILKH 190 200 210 220 230 240 IDKVSEKNIL LFGTGKIGRN TCENLVKHTR NNHITLINRT KDKAERIAGK FNLIVKDYAD 250 260 270 280 290 300 LQAEIRNSDI LIVATGAQNP TISKELIYPK KELLILDLSI PKNVSDDVHE LENVKLIHLD 310 320 330 340 350 360 HLSQMTDETL EKRKQFIPQA KEIITEVESE FNRWLETRKF APTIKALKKK LKTMKDDELD 370 380 390 400 410 FQRKKISDFN DEQAEIVSNR IIQKIMKHFA NHLKGDAETT DESLELIQKV FQLEEVNK

References

[1]

"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter." Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O. Environ. Microbiol. 8:2201-2213(2006) [PubMed: 17107561] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KT0803.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU207366 Genomic DNA. Translation: CAL68166.1.
RefSeq	YP_863233.1. NC_008571.1.
3D structure databases
ProteinModelPortal	A0M6C1.
ModBase	Search...
Protein-protein interaction databases
STRING	A0M6C1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4651311.
GenomeReviews	Gene locus GFO_3223 in contig CU207366_GR.
KEGG	gfo:GFO_3223.
NMPDR	fig|411154.5.peg.3037.
PATRIC	22075182. VBIGraFor5527_3106.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0373.
HOGENOM	HBG479062.
OMA	YADIVIS.
PhylomeDB	A0M6C1.
ProtClustDB	CLSK851822.
Enzyme and pathway databases
BioCyc	GFOR411154:GFO_3223-MONOMER.
Family and domain databases
HAMAP	MF_00087. Glu-tRNA_reductase. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_dimer. 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	PF00745. GlutR_dimer. 1 hit. PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit. [Graphical view]
PIRSF	PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAM	SSF69075. 4pyrrol_synth_GluRdtase_C. 1 hit. SSF69742. GlutR. 1 hit.
TIGRFAMs	TIGR01035. HemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_GRAFK

Accession

Primary (citable) accession number: A0M6C1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	December 12, 2006
Last modified:	December 14, 2011
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program