Q6M130 (HEM1_METMP) 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:	MMP0088

Organism

Methanococcus maripaludis (strain S2 / LL) [Complete proteome] [HAMAP]

Taxonomic identifier

267377 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanococcaceae › Methanococcus

Protein attributes

Sequence length	382 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 – 382	382	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_0000114104
Regions
	Nucleotide binding	164 – 169	6	NADP By similarity
	Region	38 – 41	4	Substrate binding By similarity
	Region	90 – 92	3	Substrate binding By similarity
Sites
	Active site	39	1	Nucleophile By similarity
	Binding site	85	1	Substrate By similarity
	Binding site	96	1	Substrate By similarity
	Site	75	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6M130 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: E73FD60D719A0C47	FASTA	382	43,612
	10 20 30 40 50 60 MLVVRADYKK YPIPVLEKMR IDEDEFYKKY DACVVVQTCN RIEAYFDTEV NSDLNCILND 70 80 90 100 110 120 FSGFDILKGK NATFHFLKVS CGMDSMILGE NQILGQIKTS FQKARELKKT SRYLDSVFLK 130 140 150 160 170 180 AIHVGQRART ETKINEGSVS IGSAAVELAE KNFGLANKNV LLIGAGEIGT LVAKALMEKH 190 200 210 220 230 240 IKAVIVANRT YERAETLAKE LKGMAVHFDK LKEAINFSDV IICATSSPHY ILKKEDLIDV 250 260 270 280 290 300 GNKIIIDIAN PRDVDDAVRE FENINLYTID DLRNISDKNL QKRIEEVPAV EKIIDEEYDV 310 320 330 340 350 360 LMKQIEKINV EEVLKDFNNY IEEIRTKELE KAIKLSKTKN PEEIMENFSK AFAKRITHDF 370 380 VSYSINTSKE DLMNSAWWKN GK

References

[1]

"Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis." Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J., Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M., Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A., Moore B.C. , Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D., Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W., Olson M.V., Leigh J.A. J. Bacteriol. 186:6956-6969(2004) [PubMed: 15466049] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: S2 / LL.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX950229 Genomic DNA. Translation: CAF29644.1.
RefSeq	NP_987208.1. NC_005791.1.
3D structure databases
ProteinModelPortal	Q6M130.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2762055.
GenomeReviews	Gene locus MMP0088 in contig BX950229_GR.
KEGG	mmp:MMP0088.
NMPDR	fig|267377.1.peg.88.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG732626.
OMA	YADIVIS.
ProtClustDB	PRK00045.
Enzyme and pathway databases
BioCyc	MMAR267377:MMP0088-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:1.10.1200.70. 4pyrrol_synth_GluRdtase_dimer. 1 hit. 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_METMP

Accession

Primary (citable) accession number: Q6M130

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	July 5, 2004
Last modified:	December 14, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program