Reviewed, UniProtKB/Swiss-Prot A8FFV4 (HEM1_BACP2)

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:	BPUM_2458

Organism

Bacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]

Taxonomic identifier

315750 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	455 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 – 455	455	Glutamyl-tRNA reductase		PRO_1000057570
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)
	A8FFV4-1 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: 8F3B7A3B560BA362	FASTA	455	50,817
	10 20 30 40 50 60 MHILVVGLDY KTAPVEIREQ LSFEPSELGT AMSKLKEEKS ILENIVISTC NRTEIYAVVD 70 80 90 100 110 120 QLHTGRFYIK RFLADWFGLE KEDVSPYLKF YENDGAVEHL FRVACGLDSM VIGETQILGQ 130 140 150 160 170 180 VRSSFKVAQE EKTIGTVFNY LFKQAVTVAK RSHAETDIAS NAVSVSYAAV ELAKKIFGRL 190 200 210 220 230 240 SDKHVLILGA GKMGELAAQN LQGQGIGQVT VINRTYEKAK ELAGRFSGEP KSLNQLEKTL 250 260 270 280 290 300 SEADILISST GAKQFVITKE MVESANKKRK GRPLFMVDIA VPRDLDPAIS EVEGAFLYDI 310 320 330 340 350 360 DDLEGIVAAN LKERRAVAEQ VELLIEAEIV EFKQWLNTLG VVPVISALRE KALTIQADTM 370 380 390 400 410 420 QSIERKLPNL THREMKLLNK HTKSIINQML KDPILKAKEI AAEPNAEEKL LLFKEIFDLQ 430 440 450 VEDEEQKVEP VQVEQGSFQL FKPNMAQGFA TVASE

References

[1]

"Paradoxical DNA repair and peroxide resistance gene conservation in Bacillus pumilus SAFR-032." Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C. , Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., Weinstock G.M. PLoS ONE 2:E928-E928(2007) [PubMed: 17895969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000813 Genomic DNA. Translation: ABV63121.1.
RefSeq	YP_001487681.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5621727.
GenomeReviews	Gene locus BPUM_2458 in contig CP000813_GR.
KEGG	bpu:BPUM_2458.
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_BACP2

Accession

Primary (citable) accession number: A8FFV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	November 13, 2007
Last modified:	November 25, 2008
This is version 10 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)