ID   HIS8_BIFLO              Reviewed;         386 AA.
AC   Q8G4S8;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=BL1296;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN25097.1; -; Genomic_DNA.
DR   RefSeq; NP_696461.1; NC_004307.2.
DR   RefSeq; WP_011067977.1; NC_004307.2.
DR   AlphaFoldDB; Q8G4S8; -.
DR   SMR; Q8G4S8; -.
DR   STRING; 206672.BL1296; -.
DR   EnsemblBacteria; AAN25097; AAN25097; BL1296.
DR   KEGG; blo:BL1296; -.
DR   PATRIC; fig|206672.9.peg.145; -.
DR   HOGENOM; CLU_017584_3_1_11; -.
DR   OMA; IWLNANE; -.
DR   PhylomeDB; Q8G4S8; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000000439; 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   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..386
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153316"
FT   MOD_RES         240
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   386 AA;  42535 MW;  CCFE6B34B853AA3A CRC64;
     MSSIPANLPL RNDLIGEEPY GAPQLDVPVC LNVNENPYAP DPAVCDTIAK RVREIAPTLN
     RYPDREHIEL RQAFSDYLAR ESGTRLDVDE LWGANGSNEI MLQLFQAFGG PGRTALGADP
     TYSMYPEYAR DTFTGWKLAH RNADFTLNVD KVLEAIAEVK PSMVLLTSPN NPTGTPLPME
     DIERILAACE TAEVVGAGEG VHPILVIDEA YVEFRKPGTP SAVSLIKDHP NLAVSRTMSK
     AFAFAGARVG YLAASKGIID CVRIVRMPYH LSAVTQAAAL AAFEHADEQL SRVEHLRETR
     EATAAWLKEQ TYKDQPLEVA ESGSNFLLFG GHFDKREAIF DELLKRGVLI RVVGPDGWLR
     VCMGTDEEME TFRNALVEVL RIVEAA