Q12WM5 (HEM1_METBU) 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:	Mbur_1229

Organism

Methanococcoides burtonii (strain DSM 6242) [Complete proteome] [HAMAP]

Taxonomic identifier

259564 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanococcoides

Protein attributes

Sequence length	422 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 – 422	422	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_1000004637
Regions
	Nucleotide binding	180 – 185	6	NADP By similarity
	Region	48 – 51	4	Substrate binding By similarity
	Region	105 – 107	3	Substrate binding By similarity
Sites
	Active site	49	1	Nucleophile By similarity
	Binding site	100	1	Substrate By similarity
	Binding site	111	1	Substrate By similarity
	Site	90	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q12WM5 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: A7621706C2763CE2	FASTA	422	47,205
	10 20 30 40 50 60 MTEISSMVIT HAKATVEEME DSWHGDIDLV LSQLYSNELV YECAVLKTCN RVEIYVVSSK 70 80 90 100 110 120 GSSVLFHYAK EMGVSAKIVE FYDHDESLRH LLRLACGLES MIIGEDQILG QIKDFFLMAK 130 140 150 160 170 180 GAGTVGKVLS TAFSKAIQVG KRVRTETFIN RGAVSIASAA VDLAEDILDG LNDKHILVIG 190 200 210 220 230 240 TGEMGTLVTR ALSHRDMHVI YLANRTYEKA RDLAEELGGE AVMFDQLEKY VRAADVVISA 250 260 270 280 290 300 TSAPHYVLKG DLVAKVMEGR ENELLLIDIA SPRDIDPAVE EIPHVILRNI DGLRVINEKN 310 320 330 340 350 360 LQMRMVEAKK AEIIIDDELD MVKAQYKRQK ADAIISNLYS QSHGLRHNEM EHAINKLSAY 370 380 390 400 410 420 HTIGEIERKV LEDLTHAITN KILAEPTKKL RNAAEYDDDK FLDSVSRLFD IRPIKKNDGI TK

References

[1]

"Complete sequence of Methanococcoides burtonii DSM 6242." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Anderson I., Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., Richardson P. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 6242.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000300 Genomic DNA. Translation: ABE52151.1.
RefSeq	YP_565901.1. NC_007955.1.
3D structure databases
ProteinModelPortal	Q12WM5.
ModBase	Search...
Protein-protein interaction databases
STRING	Q12WM5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3998553.
GenomeReviews	Gene locus Mbur_1229 in contig CP000300_GR.
KEGG	mbu:Mbur_1229.
NMPDR	fig|259564.8.peg.1164.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG04783.
HOGENOM	HBG732626.
OMA	YADIVIS.
PhylomeDB	Q12WM5.
ProtClustDB	PRK00045.
Enzyme and pathway databases
BioCyc	MBUR259564:MBUR_1229-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_METBU

Accession

Primary (citable) accession number: Q12WM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	August 22, 2006
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program