HIS8_BACTN
ID HIS8_BACTN Reviewed; 346 AA.
AC Q8ABA8;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01023};
DE EC=2.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01023};
DE AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000255|HAMAP-Rule:MF_01023};
GN Name=hisC {ECO:0000255|HAMAP-Rule:MF_01023}; OrderedLocusNames=BT_0202;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-
CC oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766,
CC ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01023};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01023};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC {ECO:0000255|HAMAP-Rule:MF_01023}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01023}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01023}.
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DR EMBL; AE015928; AAO75309.1; -; Genomic_DNA.
DR RefSeq; NP_809115.1; NC_004663.1.
DR RefSeq; WP_008766231.1; NC_004663.1.
DR AlphaFoldDB; Q8ABA8; -.
DR SMR; Q8ABA8; -.
DR STRING; 226186.BT_0202; -.
DR PaxDb; Q8ABA8; -.
DR PRIDE; Q8ABA8; -.
DR EnsemblBacteria; AAO75309; AAO75309; BT_0202.
DR GeneID; 60926166; -.
DR KEGG; bth:BT_0202; -.
DR PATRIC; fig|226186.12.peg.200; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_1_10; -.
DR InParanoid; Q8ABA8; -.
DR OMA; IWLNANE; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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; Histidine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..346
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_0000153314"
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ SEQUENCE 346 AA; 39729 MW; 14021C6FC73F924B CRC64;
MKTLQELTRP NIWKLKPYSS ARDEYKGAVA SVFLDANENP YNLPHNRYPD PMQWELKTLL
SKIKKVSPQH IFLGNGSDEA IDLVFRAFCE PEKDNVVAID PTYGMYQVCA DVNNVEYRKV
LLDENFQFSA EKLLAATDER TKLIFLCSPN NPTGNDLLRS EIEKILREFE GLVILDEAYN
DFSEAPSFLE ELDKYPNLVV FQTFSKAWGC AAIRLGMAFA SEAIIGILSK IKYPYNVNQL
TQQQAIAMLH KYYEIERWIK TLKEERDYLE EEFAKLSCTV RMYPSDSNFF LAKVTDAVKI
YNYLVGEGII VRNRHSISLC CNCLRVTVGT RVENNTLLAA LKKYQG