Reviewed, UniProtKB/Swiss-Prot A6TJD3 (HEM1_ALKMQ)

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:	Amet_0058

Organism

Alkaliphilus metalliredigens (strain QYMF) [Complete proteome] [HAMAP]

Taxonomic identifier

293826 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Alkaliphilus

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	L-glutamate 1-semialdehyde + NADP(+) + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Subunit structure	Homodimer By similarity.
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.
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.
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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW porphyrin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: HAMAP shikimate 5-dehydrogenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 424	424	Glutamyl-tRNA reductase		PRO_1000057567
Regions
	Nucleotide binding	189 – 194	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	114 – 116	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	109	1	Substrate By similarity
	Binding site	120	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6TJD3-1 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: AFB0A1080D7E55C1	FASTA	424	48,297
	10 20 30 40 50 60 MKIIVFGITH KKATIDLREK VAFSQSKKQE AYSLLKESPF IHEAVILSTC NRSEVFAVVQ 70 80 90 100 110 120 DTSIARRWFK RFYTDFFQLK ETALEGCNHF EKGREAVQYL YHVCVGVDSL VIGEDQILGQ 130 140 150 160 170 180 VKEAHAEALD FAATGKILNK LFLEAVTTAK EVKTETAISE NALSISSIAV KQMENHLKGL 190 200 210 220 230 240 VGKTVLVVGF GKMSRIAIEN LLCKGIKRLY ICNRTKESVQ ELIEKHPQIH YLSYDQKYEM 250 260 270 280 290 300 LNGVDAVISA TGAPHFIFYK EDMEKIYQKH RPMCMIDIAL PRDIDPAVKE IEGIELFHID 310 320 330 340 350 360 DLKEIANENL AYRMDCIEII KQSINEAIEK YEGWYQCLPI YPRIQAIKAY SETLTDQELE 370 380 390 400 410 420 KLFKRLDHMA EEDRQVIEVV VKSLVKKMWK TPILQLKDAG IRGNGEAFAA FVDEFLGLDA GCGK

References

[1]

"Complete sequence of Alkaliphilus metalliredigens QYMF." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J., Fields M., Richardson P. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000724 Genomic DNA. Translation: ABR46301.1.
RefSeq	YP_001317960.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5310101.
GenomeReviews	Gene locus Amet_0058 in contig CP000724_GR.
KEGG	amt:Amet_0058.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_00087. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_C. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR016040. NAD(P)-bd. IPR006151. Shikm_DHase/Glu-tRNA_Rdtase. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
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.
TIGRFAMs	TIGR01035. hemA. 1 hit.
PROSITE	PS00747. GLUTR. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_ALKMQ

Accession

Primary (citable) accession number: A6TJD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	August 21, 2007
Last modified:	November 25, 2008
This is version 13 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)