A9WPH1 (HEM1_RENSM) 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:	RSal33209_1218

Organism

Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235) [Complete proteome] [HAMAP]

Taxonomic identifier

288705 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Renibacterium

Protein attributes

Sequence length	440 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 – 440	440	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_0000335064
Regions
	Nucleotide binding	181 – 186	6	NADP By similarity
	Region	40 – 43	4	Substrate binding By similarity
	Region	105 – 107	3	Substrate binding By similarity
Sites
	Active site	41	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)
	A9WPH1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: D97066F78C188072	FASTA	440	45,781
	10 20 30 40 50 60 MNVVVLFSLV ATHADIDLET VARLSAGSAA VSTSTVVLAT CNRFEIYSAA ENPATARAEM 70 80 90 100 110 120 EAALAHATGF APSLVSSSFK LLTGTDVAKH LFAVASGLDS AVVGEREIAG QVRRALIDAQ 130 140 150 160 170 180 TAFPVPGPLV RLFQTASRTA KDVGSQTALG SQGRSIVSVA LDLAGDSSAT AWDQRKAVVF 190 200 210 220 230 240 GTGAYAGVTM ALLRERGVSD LSVYSSSGRA ADFVASRGGT AAESLEEALG SADLVIGCSG 250 260 270 280 290 300 SDQRVSAETL ADIRRRTGTA GEPLSVIDLA LSRDFDPAIT ELPGVELLTL ETVRLAAPSE 310 320 330 340 350 360 QESALLQTQV IVSRAAADFE LSIATRSVDT AIVALRKHTM AVLDAEMERV RAQHGCTAAA 370 380 390 400 410 420 EEVEFALRRM VKQLLHGPTV RARELAAAGQ QAEYIAALQS LYGIELESPT PAAQPVESIP 430 440 AVEPASCPVN HNAVDRSQSA

References

[1]

"Genome sequence of the fish pathogen Renibacterium salmoninarum suggests reductive evolution away from an environmental Arthrobacter ancestor." Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S. J. Bacteriol. 190:6970-6982(2008) [PubMed: 18723615] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000910 Genomic DNA. Translation: ABY22956.1.
RefSeq	YP_001624370.1. NC_010168.1.
3D structure databases
ProteinModelPortal	A9WPH1.
ModBase	Search...
Protein-protein interaction databases
STRING	A9WPH1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5822473.
GenomeReviews	Gene locus RSal33209_1218 in contig CP000910_GR.
KEGG	rsa:RSal33209_1218.
PATRIC	23075677. VBIRenSal21953_1259.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG732626.
OMA	AYAGATM.
ProtClustDB	PRK00045.
Enzyme and pathway databases
BioCyc	RSAL288705:RSAL33209_1218-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.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_RENSM

Accession

Primary (citable) accession number: A9WPH1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program