Reviewed, UniProtKB/Swiss-Prot Q81LC5 (HEM1_BACAN)

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:	BA_4698, GBAA4698, BAS4363

Organism

Bacillus anthracis [Complete proteome] [HAMAP]

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	444 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 – 444	444	Glutamyl-tRNA reductase		PRO_0000113988
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)
	Q81LC5-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 4BB7F3FC998B0643	FASTA	444	49,825
	10 20 30 40 50 60 MHILVVSVNY RTAPVEFREK LTFQAAELER AMTTLQNQKS VLENVIVSTC NRTEIYAVVD 70 80 90 100 110 120 QLHTGRYYIK KFLADWFQLE IEEVAPYLTI FEQDGAIDHL FRVTCGLDSM VVGETQILGQ 130 140 150 160 170 180 IKDSFLEAQQ VKATGTIFNE LFKQVITLAK RAHSETTIGE SAMSVSYAAV ELGKKIFGEL 190 200 210 220 230 240 TDCHVLILGA GKMGELALQN LYGSGARKVT VMNRTLSKAE IMAEKYMGHA KPLSELQCAL 250 260 270 280 290 300 LEADILISST GASDYVITKE MMTKVEKMRS GRPLFMVDIA VPRDIDPAID ELEGSFLYDI 310 320 330 340 350 360 DDLQGVVEAN RAERLKEAEK IQFMIEEEIV LFKTWLSTLG VVPLISALRD KALAIQSETM 370 380 390 400 410 420 ESLERKIPNL SDRERKVISK HTKSIINQLL KDPILVAKEI AAEEGADEKL ALFAKIFDLE 430 440 MEDVESRAEE VEHKRVWTPS VPSL

References

[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016879 Genomic DNA. Translation: AAP28397.1. AE017334 Genomic DNA. Translation: AAT33821.1. AE017225 Genomic DNA. Translation: AAT56661.1.
RefSeq	NP_846911.1. YP_021346.1. YP_030610.1.
3D structure databases
HSSP	HSSP built from PDB template 1GPJ based on UniProtKB Q9UXR8.
ModBase	Search...
Genome annotation databases
GeneID	1083700. 2816103. 2852284.
GenomeReviews	Gene locus BA_4698 in contig AE016879_GR. Gene locus BAS4363 in contig AE017225_GR. Gene locus GBAA4698 in contig AE017334_GR.
KEGG	ban:BA4698. bar:GBAA4698. bat:BAS4363.
TIGR	BA_4698. GBAA4698.
Phylogenomic databases
HOGENOM	Q81LC5.
Enzyme and pathway databases
BioCyc	BANT260799:BAS4363-MON. BANT261594:GBAA4698-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_BACAN

Accession

Primary (citable) accession number: Q81LC5
Secondary accession number(s): Q6HSS8, Q6KM21

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	June 1, 2003
Last modified:	November 25, 2008
This is version 48 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)