Reviewed, UniProtKB/Swiss-Prot Q2KZZ5 (HEM1_BORA1)

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:	BAV0296

Organism

Bordetella avium (strain 197N) [Complete proteome] [HAMAP]

Taxonomic identifier

360910 [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. 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 – 424	424	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_0000335012
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)
	Q2KZZ5-1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: 87B2847C69F13B8E	FASTA	424	46,254
	10 20 30 40 50 60 MSVAVLAFGL NHTSAPVSVR ERVSMPVDLV KPALAGLRSA FGGAVREAAI LSTCNRTEVY 70 80 90 100 110 120 CAADAAVAEQ LPIWLADHHC MEAGSLHPHL YRLHQNDAVR HAFRVASGLD SMVLGEPQIL 130 140 150 160 170 180 GQMKDAVRAA EEAGSLGTLL HQLFQRTFAV AKEVRSQTEI GAHSVSMAAA AVRLAERVFG 190 200 210 220 230 240 DLGQARTLFI GAGEMIELCA THFAAQHPRS MVVANRTAER AESLAGRFSA GTMKLADLTE 250 260 270 280 290 300 RLAEFDVVVS CTASSLPILG LGMVERATRQ RRHRPMVMID LAVPRDIEPE VGRLDDVYLY 310 320 330 340 350 360 SVDDLGRLVQ SGTDARRAAV VQAEAIIETR VQGFMHWMQS REVVPVIRGL HQAAEDVQAA 370 380 390 400 410 420 ELERARRLLA RGESPEAVLE QLAHGLTQKY LHGPLAALNR SAGDERKQLL AWMPRLFPGR DSRR

References

[1]

"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction." Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M. J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM167904 Genomic DNA. Translation: CAJ47901.1.
RefSeq	YP_784834.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	6267876.
GenomeReviews	Gene locus BAV0296 in contig AM167904_GR.
KEGG	bav:BAV0296.
NMPDR	fig|521.1.peg.1136.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2KZZ5.
OMA	Q2KZZ5. 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_BORA1

Accession

Primary (citable) accession number: Q2KZZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	March 7, 2006
Last modified:	June 16, 2009
This is version 33 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)