Reviewed, UniProtKB/Swiss-Prot A0RNT0 (HEM1_CAMFF)

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:	CFF8240_0688

Organism

Campylobacter fetus subsp. fetus (strain 82-40) [Complete proteome] [HAMAP]

Taxonomic identifier

360106 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	422 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. 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.
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 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 HAMAP MF_00087		PRO_1000057571
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)
	A0RNT0-1 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: 9A2B9A3FE3EC3FAB	FASTA	422	47,142
	10 20 30 40 50 60 MHYVSISFTH KNTDIGVREK LSFSDNNRRR EILRLIGAND SIAESMALST CNRVEIFAYV 70 80 90 100 110 120 LDTQSSIRHI LNSISILTLV PFEALELRAD IYEDQGAIHH LFAVASSLDS LVVGETQIAG 130 140 150 160 170 180 QLKEAFKFAY DNEDCGVNIS SAMHFAFKCA AEVRALTTIS KNPVSVSSVA VAKAKEIYGN 190 200 210 220 230 240 IGGMSAVVIG AGEMSRLAAQ HLINAEVNVI IINRDEIKAQ TLAKELGELA SYASFDKLSE 250 260 270 280 290 300 YINRYRLIFS ATGAPNAIIT NEIIEQKDFH RYFFDIAVPR DIDIEEDEYI HVYAVDDLEE 310 320 330 340 350 360 IVRTNLALRE EQASIAYSIV GKSTTSFFKW RLSEGSTPAI KALRLKAKDI ACKEIEKAVK 370 380 390 400 410 420 KGYLKCSDQD EASKLVHQVF KAFLHTPSVR LKEKNSDDIL KALEYLFDIK IQKDENLEGN LK

References

[1]	"Sequence of Campylobacter fetus subsp. fetus 82-40." Fouts D.E., Nelson K.E. Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000487 Genomic DNA. Translation: ABK82043.1.
RefSeq	YP_891863.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4539153.
GenomeReviews	Gene locus CFF8240_0688 in contig CP000487_GR.
KEGG	cff:CFF8240_0688.
NMPDR	fig|360106.5.peg.651.
TIGR	CFF8240_0688.
Phylogenomic databases
OMA	A0RNT0. GPILNRL.
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_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

HEM1_CAMFF

Accession

Primary (citable) accession number: A0RNT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	January 9, 2007
Last modified:	June 16, 2009
This is version 24 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)