Reviewed, UniProtKB/Swiss-Prot Q2IJD4 (HEM11_ANADE)

Names and origin

Protein names

Recommended name:
    Glutamyl-tRNA reductase 1
      Short name=GluTR 1
    EC=1.2.1.70

Gene names

Name:	hemA1
Ordered Locus Names:	Adeh_1994

Organism

Anaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]

Taxonomic identifier

290397 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Anaeromyxobacter

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	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 or NADPH 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 – 422	422	Glutamyl-tRNA reductase 1 HAMAP MF_00087		PRO_0000335005
Regions
	Nucleotide binding	183 – 188	6	NADP By similarity
	Region	48 – 51	4	Substrate binding By similarity
	Region	108 – 110	3	Substrate binding By similarity
Sites
	Active site	49	1	Nucleophile By similarity
	Binding site	103	1	Substrate By similarity
	Binding site	114	1	Substrate By similarity
	Site	93	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2IJD4-1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: B2F7050D3958C325	FASTA	422	44,435
	10 20 30 40 50 60 MLVAVGLNQK GATVADREVL ALPSEELLDA LTAFQALDGV DEVAIVSTCY RVEIFAAARC 70 80 90 100 110 120 PAAAELSLRH ALEARAGRSL PLFELQGEEA FRHLVRVASS LESAILGEPQ ILGQVKDAFH 130 140 150 160 170 180 RAAEAGAAGK ELASVLSRAL AAAKRVRTET AVGRAGVSWG NAAAALASKV LGPLAGRRVA 190 200 210 220 230 240 VIGAGEMARL TAQHMRDERA SVVVLNRTLA NAEALAAEVG GEARPLDALE QELLRADVVV 250 260 270 280 290 300 SAAPAAPAAL APAVMQRILH ARRKRIVMVD LAVPRAIPAE TGALPDVYLC DVDDLDRVMK 310 320 330 340 350 360 AAMAERAQAA QHAERIADEE VQKFARAEAE RRAAPLIQEM RSRASAIARE EVERTLRRLG 370 380 390 400 410 420 EDPELAKRLD AMAGSIVSKI LHAPSTRLRQ AVCDGGANDP LVAAAVQIFD LSAAPAARGD AA

References

[1]

"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000251 Genomic DNA. Translation: ABC81764.1.
RefSeq	YP_465201.1.
3D structure databases
SMR	Q2IJD4. Positions 2-412.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2IJD4.
Genome annotation databases
GeneID	3887141.
GenomeReviews	Gene locus Adeh_1994 in contig CP000251_GR.
KEGG	ade:Adeh_1994.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0373.
HOGENOM	HBG732626.
OMA	IICATSS.
PhylomeDB	Q2IJD4.
Enzyme and pathway databases
BioCyc	ADEH290397:ADEH_1994-MONOMER.
Family and domain databases
HAMAP	MF_00087. Glu-tRNA_reductase. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_C. 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.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM11_ANADE

Accession

Primary (citable) accession number: Q2IJD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	March 7, 2006
Last modified:	February 9, 2010
This is version 39 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)