Q5YP69 (HEM1_NOCFA) 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:	NFA_51700

Organism

Nocardia farcinica (strain IFM 10152) [Complete proteome] [HAMAP]

Taxonomic identifier

247156 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Nocardia

Protein attributes

Sequence length	477 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 – 477	477	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_0000335054
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
	Site	99	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5YP69 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: ECD6A35672A88F32	FASTA	477	50,016
	10 20 30 40 50 60 MSVLLVGVSH RSAPVSVLEK VAITDADRPK LIDKMLASSH ISEAMIVSTC NRVEVYAVVD 70 80 90 100 110 120 AFHGGLAEVG ELLTRHSGLA MPDLTKHAYV RYSEAAAEHL FAVASGLDSM VVGEQQVLSQ 130 140 150 160 170 180 IRGAYATADA QQAVGRTLHE LAQHALRVGK RVHSETGIDR AGASVVSVAL DRAAQVLGDL 190 200 210 220 230 240 AGRTAVVVGA GAMGGLSVAH LARAGIGRII VVNRTIERAR RLAETAASYG VESSALELDR 250 260 270 280 290 300 LHEAMSAADV VLSCTGAVGA VVTLADTHRA LADRDRAEFP AGDRPLVFCD LGLPRDVEPA 310 320 330 340 350 360 VAGLPGVAVI DIESLQRDPA AGAAADDTAA ARSIVAEELA KYLAGQRMAE VTPTVAALRQ 370 380 390 400 410 420 RAAEVVEAEL LRLDSRLPGL AEPERDEVAR TVRRVVDKLL HAPTVRVKQL ASTPGGDSYA 430 440 450 460 470 EALRELFELK PGAAQAVAAP MEITAIGPDR TAGLADDFTP GHRLDFEQHL GEEGKPA

References

[1]

"The complete genomic sequence of Nocardia farcinica IFM 10152." Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K., Shiba T., Hattori M. Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004) [PubMed: 15466710] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IFM 10152.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP006618 Genomic DNA. Translation: BAD60022.1.
RefSeq	YP_121386.1. NC_006361.1.
3D structure databases
HSSP	HSSP built from PDB template 1GPJ based on UniProtKB Q9UXR8.
ProteinModelPortal	Q5YP69.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3109557.
GenomeReviews	Gene locus NFA_51700 in contig AP006618_GR.
KEGG	nfa:nfa51700.
NMPDR	fig|247156.1.peg.4968.
PATRIC	22739927. VBINocFar94200_5182.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG732626.
OMA	KETIFRR.
ProtClustDB	PRK00045.
Enzyme and pathway databases
BioCyc	NFAR247156:NFA51700-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_NOCFA

Accession

Primary (citable) accession number: Q5YP69

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	November 23, 2004
Last modified:	January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program