Q81P62 (HIS82_BACAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidinol-phosphate aminotransferase 2
EC=2.6.1.9

Alternative name(s):
Imidazole acetol-phosphate transaminase 2

Gene names

Name:	hisC2
Synonyms:	hisC-2
Ordered Locus Names:	BA_2955, GBAA_2955, BAS2746

Organism

Bacillus anthracis

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	366 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. HAMAP MF_01023
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_01023
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP MF_01023
Subunit structure	Homodimer By similarity. HAMAP MF_01023
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC histidinol-phosphate transaminase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding 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 – 366	366	Histidinol-phosphate aminotransferase 2 HAMAP MF_01023		PRO_0000153298
Amino acid modifications
	Modified residue	222	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q81P62 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 784AEB1703E7482E	FASTA	366	41,112
	10 20 30 40 50 60 MQVKDQLSSL QPYKPGKSPE QMKEVYGDHS FVKLASNENP FGCSPRVLDE LQKSWLDHAL 70 80 90 100 110 120 YPDGGATTLR QTIANKLHVK MEQVLCGSGL DEVIQMISRA VLKAGDNIVT AGATFPQYRH 130 140 150 160 170 180 HAIIEGCEVK EVALNNGVYD LDEISSVVDN DTKIVWICNP NNPTGTYVND RKLTQFIEGI 190 200 210 220 230 240 SENTLIVIDE AYYEYVTAKD FPETLPLLEK HKNILVLRTF SKAYGLASFR VGYAVGHEEL 250 260 270 280 290 300 IEKLNVVRLP FNVSSLAQKA ATIAFGDDEF IEEIVRVNTE GLRQYESFCK ENEIPFYQSQ 310 320 330 340 350 360 TNFIFLPVEN GGEIYEACAH AGFIIRPFPN GVRITVGTRE QNEGVISVLQ QHFENKKRKS RDEANA

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016879 Genomic DNA. Translation: AAP26776.1. AE017334 Genomic DNA. Translation: AAT70137.1. AE017225 Genomic DNA. Translation: AAT55055.1.
RefSeq	NP_845290.1. NC_003997.3. YP_029004.1. NC_005945.1. YP_052629.1. NC_007530.2.
3D structure databases
ProteinModelPortal	Q81P62.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000010820; EBBACP00000010576; EBBACG00000010812. EBBACT00000018514; EBBACP00000018135; EBBACG00000018505. EBBACT00000022072; EBBACP00000021557; EBBACG00000022063.
GeneID	1088520. 2821170. 2852549.
GenomeReviews	Gene locus BA_2955 in contig AE016879_GR. Gene locus BAS2746 in contig AE017225_GR. Gene locus GBAA_2955 in contig AE017334_GR.
KEGG	ban:BA_2955. bar:GBAA_2955. bat:BAS2746.
TIGR	BA_2955. GBAA_2955.
Phylogenomic databases
GeneTree	EBGT00050000000787.
HOGENOM	HBG646350.
OMA	NNTKIVW.
ProtClustDB	PRK01533.
Enzyme and pathway databases
BioCyc	BANT260799:BAS2746-MONOMER. BANT261594:GBAA2955-MONOMER.
Family and domain databases
HAMAP	MF_01023. HisC_aminotrans_2. [Tree]
InterPro	IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KO	K00817.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01141. HisC. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS82_BACAN

Accession

Primary (citable) accession number: Q81P62
Secondary accession number(s): Q6HXD4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	June 1, 2003
Last modified:	November 16, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program