ID A9VMC7_BACWK Unreviewed; 370 AA.
AC A9VMC7;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 01-MAY-2013, entry version 41.
DE RecName: Full=Histidinol-phosphate aminotransferase;
DE EC=2.6.1.9;
DE AltName: Full=Imidazole acetol-phosphate transaminase;
GN Name=hisC; OrderedLocusNames=BcerKBAB4_1442;
OS Bacillus weihenstephanensis (strain KBAB4).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBAB4;
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B.,
RA Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.H.,
RA Sanchis V., Nguen-The C., Lereclus D., Richardson P., Wincker P.,
RA Weissenbach J., Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
CC -!- CATALYTIC ACTIVITY: L-histidinol phosphate + 2-oxoglutarate = 3-
CC (imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate.
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily.
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DR EMBL; CP000903; ABY42689.1; -; Genomic_DNA.
DR RefSeq; YP_001644317.1; NC_010184.1.
DR ProteinModelPortal; A9VMC7; -.
DR STRING; 315730.BcerKBAB4_1442; -.
DR EnsemblBacteria; ABY42689; ABY42689; BcerKBAB4_1442.
DR GeneID; 5841656; -.
DR KEGG; bwe:BcerKBAB4_1442; -.
DR PATRIC; 19007422; VBIBacWei55973_2030.
DR eggNOG; COG0079; -.
DR HOGENOM; HOG000288510; -.
DR KO; K00817; -.
DR OMA; YIELADI; -.
DR ProtClustDB; PRK03158; -.
DR BioCyc; BWEI315730:GHRU-1559-MONOMER; -.
DR UniPathway; UPA00031; UER00012.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:HAMAP.
DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01023; HisC_aminotrans_2; 1; -.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR005861; HisP_aminotrans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR TIGRFAMs; TIGR01141; hisC; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW Histidine biosynthesis; Pyridoxal phosphate; Transferase.
FT MOD_RES 222 222 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 370 AA; 41501 MW; 6067C8151181C8D4 CRC64;
MRVKEQLLTL RAYVPGKNIE EVKREYGLSK IVKLASNENP FGCSARVTEA LTSLANQYAL
YPDGAAFELR EKVAEHLGVK AEQLLFGSGL DEVIQMISRA LLHNGTNVVM ANPTFSQYHH
HAVIEGAEVR EVPLKDGIHD LDAMLQQVDE KTKIVWVCNP NNPTGTYVEK QKLLSFLESV
PKSALVIMDE AYYEYAGAED YPQTLPLLEK YENLMVLRTF SKAYGLAAFR IGYAIGDAKL
IGQLEVARLP FNTSTIAQAV ALAAIEDQQF LQECVKKNAG GLNQYYAFCK EYNVFYYPSQ
TNFIFLKLGI PGNEAFERLM KKGYIVRSGA AFGMHDGIRI TVGLKEENDE IIELLTELVK
EQVKKEETYS
//
