ID HIS81_BACCR Reviewed; 370 AA.
AC Q81FQ1;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 12-APR-2017, entry version 91.
DE RecName: Full=Histidinol-phosphate aminotransferase 1;
DE EC=2.6.1.9;
DE AltName: Full=Imidazole acetol-phosphate transaminase 1;
GN Name=hisC1; OrderedLocusNames=BC_1518;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 /
OS NCIMB 9373 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL
RC B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B.,
RA Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A.,
RA Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T.,
RA Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D.,
RA Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with
RT Bacillus anthracis.";
RL Nature 423:87-91(2003).
CC -!- CATALYTIC ACTIVITY: L-histidinol phosphate + 2-oxoglutarate = 3-
CC (imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000305}.
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DR EMBL; AE016877; AAP08498.1; -; Genomic_DNA.
DR RefSeq; NP_831297.1; NC_004722.1.
DR RefSeq; WP_001264019.1; NC_004722.1.
DR ProteinModelPortal; Q81FQ1; -.
DR SMR; Q81FQ1; -.
DR STRING; 226900.BC1518; -.
DR PRIDE; Q81FQ1; -.
DR EnsemblBacteria; AAP08498; AAP08498; BC_1518.
DR GeneID; 1203867; -.
DR KEGG; bce:BC1518; -.
DR PATRIC; 32598772; VBIBacCer54481_1495.
DR eggNOG; COG0079; LUCA.
DR KO; K00817; -.
DR OMA; YPSEANY; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
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_sub2.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 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; Reference proteome;
KW Transferase.
FT CHAIN 1 370 Histidinol-phosphate aminotransferase 1.
FT /FTId=PRO_0000153301.
FT MOD_RES 222 222 N6-(pyridoxal phosphate)lysine.
FT {ECO:0000250}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 2 359 ihamap:HisC_aminotrans_2 [T]
FT MYHIT 30 352 ipfam:Aminotran_1_2 [T]
FT MYHIT 219 228 ipat:AA_TRANSFER_CLASS_2 [T]
SQ SEQUENCE 370 AA; 41620 MW; 5CF1BD42152BC048 CRC64;
MRVKEQLLTL RAYVPGKNIE EVKREYGLSK IVKLASNENP FGCSARVTEA LTSLASQYAL
YPDGYAFELR TKIAEHLGVK AEQLLFGSGL DEVIQMISRA LLHEGTNVVM ANPTFSQYHH
HAVIEGAEVR EVSLKDGIHD LDAMLEQVDE KTKIVWICNP NNPTGTYVEK QKLLSFLESV
PKSALVIMDE AYYEYAEAED YPQTLPLLEK YENLMVLRTF SKAYGLAAFR IGYAIGDAKL
IGQLEVARLP FNTSTVAQSV ALAALEDQAF LQDCVQKNAE GLNQYYAFCK EYNVFYYPSQ
TNFIFLKLGI PGNEAFERLM KKGYIVRSGA AFGIDDGIRI TVGLKEENDE IIELLKELVN
EQVQKEETYS
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