Q8TT60 (HEM1_METAC) 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:	MA_0577

Organism

Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)

Taxonomic identifier

188937 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	460 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 Reference 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 – 460	460	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_0000114100
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)
	Q8TT60 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: E239B81D1E4B6FD8	FASTA	460	51,452
	10 20 30 40 50 60 MTEISSMVIS HKKAKIEEME SAWHGDLDGL LNNLYHHEYV YECVVLKTCN RVEIYVVSPK 70 80 90 100 110 120 SSSVLFSFAK EMGASTHIID FYGHDESLEH LLRLAGGLES MIVGEDQILG QIKDLYAYSK 130 140 150 160 170 180 KAGTTGKILD TAFEKAIQVG KRIRNETRIN KGSVSIGSAA VDLAEDIFGG LTGKSVLVIG 190 200 210 220 230 240 AGEIGVLVAK ALAEKDIEAI YIANRTFKKA EEIAYELGGY AVRLDDIRGH LPDADVVISG 250 260 270 280 290 300 TGAPHYILTR EMIEEALDGR ERKLLLIDIA NPRDIEESVA ELENVELCNI DNLRVISERT 310 320 330 340 350 360 LKMRKEEAKK AEAIIQEEIR LLNIQYKRQK ADRLISELYR QVYDVRVRER EKAVNRLSAY 370 380 390 400 410 420 HTIGEIETEV LDDLTHSIVN KILAEPTKVL RQAAELGNEE FLDVVSRVFC LEKDKAKLEK 430 440 450 460 INQAKFEQIE PGCAKEQAAV KEQTAVKEQA VVKEQAAVKD

References

[1]

"The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity." Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P. , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B. Genome Res. 12:532-542(2002) [PubMed: 11932238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE010299 Genomic DNA. Translation: AAM04021.1.
RefSeq	NP_615541.1. NC_003552.1.
3D structure databases
ProteinModelPortal	Q8TT60.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1472469.
GenomeReviews	Gene locus MA_0577 in contig AE010299_GR.
KEGG	mac:MA0577.
NMPDR	fig|188937.1.peg.567.
Phylogenomic databases
HOGENOM	HBG732626.
OMA	PESSHAT.
ProtClustDB	PRK00045.
Enzyme and pathway databases
BioCyc	MACE188937:MA0577-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_METAC

Accession

Primary (citable) accession number: Q8TT60

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	June 1, 2002
Last modified:	December 14, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program