Reviewed, UniProtKB/Swiss-Prot A7I1R7 (HEM1_CAMHC)

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:	CHAB381_0896

Organism

Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A) [Complete proteome] [HAMAP]

Taxonomic identifier

360107 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	429 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 – 429	429	Glutamyl-tRNA reductase		PRO_1000057572
Regions
	Nucleotide binding	190 – 195	6	NADP By similarity
	Region	50 – 53	4	Substrate binding By similarity
	Region	115 – 117	3	Substrate binding By similarity
Sites
	Active site	51	1	Nucleophile By similarity
	Binding site	110	1	Substrate By similarity
	Binding site	121	1	Substrate By similarity
	Site	100	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7I1R7-1 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: 24112E1047B97089	FASTA	429	47,896
	10 20 30 40 50 60 MNYMSVSFTH KNTDIIVREK LSFANDVKKR EILKLICSNK AIKECLVLST CNRVEVLAYI 70 80 90 100 110 120 DDFNYTSDYV IKAISKLSGV DFDELKERAD IYEDDGAIHH LFSVASSLDS LVVGETQIVG 130 140 150 160 170 180 QLKDAYNFAK NERKSGVMLD LAINSALKCA AVIRSKTDIS KNPISVASVA VCMAREKIGD 190 200 210 220 230 240 LGGTTAVVVG AGEMAELACK HLITHKAKVI IINRNIDHAK KLAESLGENA SIAEFSNLGE 250 260 270 280 290 300 FINKYALIFS ATGANKPIIT DLLAKPQNFK RYFFDIAVPR DIDITCDDLS EVYAVDDLEE 310 320 330 340 350 360 IVRKNLLLRE EQAQIAYSIV GRETTKFYKD LKTLSSTPII KALRNSAKKV AETELKKAIK 370 380 390 400 410 420 RGYLRHSDID EARKLIHQVF KAFLHTPTVN LKNLDENAQN DINAIAEIFG IEEDFDKFCE NSLENKNEI

References

[1]

"Complete genome sequence of Campylobacter hominis ATCC BAA-381, a commensal isolated from the human gastrointestinal tract." Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Nelson K.E. Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000776 Genomic DNA. Translation: ABS52226.1.
RefSeq	YP_001406458.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5408761.
GenomeReviews	Gene locus CHAB381_0896 in contig CP000776_GR.
KEGG	cha:CHAB381_0896.
NMPDR	fig|360107.5.peg.879.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_CAMHC

Accession

Primary (citable) accession number: A7I1R7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	September 11, 2007
Last modified:	November 25, 2008
This is version 14 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)