Q736A5 (HIS82_BACC1) 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
Ordered Locus Names:	BCE_2996

Organism

Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]

Taxonomic identifier

222523 [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
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_0000153300
Amino acid modifications
	Modified residue	222	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q736A5 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 7E12832B79B95583	FASTA	366	40,982
	10 20 30 40 50 60 MQVKDQLSSL QPYKPGKSPE QMKEVYGDHA FVKLASNENP FGCSPRVLDE LQKSWLDHAL 70 80 90 100 110 120 YPDGGATTLR QTIANKLQVQ MEQVLCGSGL DEVIQIISRA ALKAGDNIVT AGATFPQYRH 130 140 150 160 170 180 HAIIEGCEVK EVPLNNGVYD LDEISSAVNN NTKIVWICNP NNPTGTYVND RKLTQFIEGI 190 200 210 220 230 240 SENTLIVIDE AYYEYVTAKD FPETLPLLEK HKNILVLRTF SKAYGLASFR VGYAIGQEEL 250 260 270 280 290 300 IEKLNVVRLP FNVSSLAQKA ATIAFGDDEF IEEIVRVNTE GLQQYESFCK ENDIPFYPSQ 310 320 330 340 350 360 TNFIFLPVEN AGEIYEACAH AGFIIRPFPN GVRITVGTRE QNEGVISVLQ QHFENKKRKS RDEANA

References

[1]

"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10987.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017194 Genomic DNA. Translation: AAS41907.1.
RefSeq	NP_979299.1. NC_003909.8.
3D structure databases
ProteinModelPortal	Q736A5.
ModBase	Search...
Protein-protein interaction databases
STRING	Q736A5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000026358; EBBACP00000025708; EBBACG00000026349.
GeneID	2748800.
GenomeReviews	Gene locus BCE_2996 in contig AE017194_GR.
KEGG	bca:BCE_2996.
NMPDR	fig|222523.1.peg.2971.
PATRIC	18854726. VBIBacCer118379_2863.
TIGR	BCE_2996.
Phylogenomic databases
eggNOG	COG0079.
GeneTree	EBGT00050000000787.
HOGENOM	HBG646350.
OMA	NNTKIVW.
ProtClustDB	PRK01533.
Enzyme and pathway databases
BioCyc	BCER405917:BCE_2996-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_BACC1

Accession

Primary (citable) accession number: Q736A5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program