ID   HIS8_CALS4              Reviewed;         351 AA.
AC   Q8R5Q4;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, 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=Histidine transaminase {ECO:0000303|PubMed:22569339};
DE            EC=2.6.1.38 {ECO:0000269|PubMed:22569339};
DE   AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000255|HAMAP-Rule:MF_01023};
GN   Name=hisC {ECO:0000255|HAMAP-Rule:MF_01023}; OrderedLocusNames=TTE2137;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
RN   [2]
RP   CATALYTIC ACTIVITY, AND COFACTOR.
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=22569339; DOI=10.1038/msb.2012.13;
RA   Yamada T., Waller A.S., Raes J., Zelezniak A., Perchat N., Perret A.,
RA   Salanoubat M., Patil K.R., Weissenbach J., Bork P.;
RT   "Prediction and identification of sequences coding for orphan enzymes using
RT   genomic and metagenomic neighbours.";
RL   Mol. Syst. Biol. 8:581-581(2012).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-histidine = 3-(imidazol-5-yl)pyruvate + L-
CC         glutamate; Xref=Rhea:RHEA:16565, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57595, ChEBI:CHEBI:58133; EC=2.6.1.38;
CC         Evidence={ECO:0000269|PubMed:22569339};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01023,
CC         ECO:0000305|PubMed:22569339};
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; AE008691; AAM25302.1; -; Genomic_DNA.
DR   RefSeq; WP_009610408.1; NC_003869.1.
DR   AlphaFoldDB; Q8R5Q4; -.
DR   SMR; Q8R5Q4; -.
DR   STRING; 273068.TTE2137; -.
DR   EnsemblBacteria; AAM25302; AAM25302; TTE2137.
DR   KEGG; tte:TTE2137; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_1_9; -.
DR   OMA; NYHVAGF; -.
DR   OrthoDB; 1248286at2; -.
DR   BRENDA; 2.6.1.38; 6784.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000000555; Chromosome.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008110; F:L-histidine:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..351
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153468"
FT   MOD_RES         213
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   351 AA;  40031 MW;  9ACF270885813239 CRC64;
     MIENLLREEI KGFKNYEVEN VPYKYKMDAN ETPFELPEEV MKNIGDIVKS IHVNIYPDPT
     AEKLREELAR YCSVTPKNIF VGNGSDEIIH LIMLAFVDKG DTVLYPHPSF AMYSIYSKIA
     GANEIAVNLN EDYTYNVERF AEAVERYKPK LVFLCNPNNP TGSVIDEEDI IRIIEKARGI
     VIVDEAYFEF YGKTLVPYID RFENLIVLRT LSKAFGIAGL RVGYALSNGE IVKYLNLVKS
     PYNLNSLSQR IALEVLKSGV LKERVNYIIN EREKLVKELN KINGIKVYPS HANFVLCKFE
     NANDVHKRLV ERGILVRNFS NVKGLEGTLR ITVSSSDAND YLINALREIL S