Reviewed, UniProtKB/Swiss-Prot Q7WQF0 (HEM1_BORBR)

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:	BB0383

Organism

Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

518 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	424 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 – 424	424	Glutamyl-tRNA reductase		PRO_0000113997
Regions
	Nucleotide binding	191 – 196	6	NADP By similarity
	Region	53 – 56	4	Substrate binding By similarity
	Region	116 – 118	3	Substrate binding By similarity
Sites
	Active site	54	1	Nucleophile By similarity
	Binding site	111	1	Substrate By similarity
	Binding site	122	1	Substrate By similarity
	Site	101	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7WQF0-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 3E9540D9435A8A27	FASTA	424	46,736
	10 20 30 40 50 60 MSVAVLAFGL NHTSAPVSVR ERVSMPVDLV KPALEGLRAT FGGAVREAAI LSTCNRTELY 70 80 90 100 110 120 CAAEGQVAEH LPAWLAEHNR LEAAALRPHL YRHQHDDAVR HAFRVASGLD SMVLGEPQIL 130 140 150 160 170 180 GQMKDAVRAA NEAGALGTLL HQLFQRTFSV AKEVRSQTAI GAHSVSMAAA AVRLAERVFG 190 200 210 220 230 240 QLEDARTLFI GAGEMIELCA THFAAQRPRS MVVANRTIER AETLAGRFSA QTMKLADLTE 250 260 270 280 290 300 RLAEFDVIVS CTASSLPILG LGMVERATRQ RRHRPMVMID LAVPRDIEPE VGRLDDVYLY 310 320 330 340 350 360 SVDDLGRLVQ SGTDARRAAV VQAEAIIETR VQGFMHWMQS REVVPVIRDL HQAADDVRAA 370 380 390 400 410 420 ELERARRMLA RGESPEAVLE QLAHGLTQKY LHGPLAALNR SEGDERRQLL AWVPRLFPGR DSRR

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RB50 / ATCC BAA-588 / NCTC 13252.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640438 Genomic DNA. Translation: CAE30881.1.
RefSeq	NP_886932.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2663607.
GenomeReviews	Gene locus BB0383 in contig BX470250_GR.
KEGG	bbr:BB0383.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7WQF0.
Enzyme and pathway databases
BioCyc	BBRO257310:BB0383-MON.
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_BORBR

Accession

Primary (citable) accession number: Q7WQF0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	October 1, 2003
Last modified:	November 25, 2008
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)