ID   HIS8_VIBVU              Reviewed;         346 AA.
AC   Q8D8Q1;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 113.
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=VV1_2918;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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; AE016795; AAO11251.1; -; Genomic_DNA.
DR   RefSeq; WP_011080738.1; NC_004459.3.
DR   AlphaFoldDB; Q8D8Q1; -.
DR   SMR; Q8D8Q1; -.
DR   EnsemblBacteria; AAO11251; AAO11251; VV1_2918.
DR   KEGG; vvu:VV1_2918; -.
DR   HOGENOM; CLU_017584_3_1_6; -.
DR   OMA; IWLNANE; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000002275; Chromosome 1.
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; Transferase.
FT   CHAIN           1..346
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153477"
FT   MOD_RES         209
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   346 AA;  38261 MW;  1146EC8B8B696694 CRC64;
     MEKLARKSVQ KLTPYLSARR IGGTGDVWLN ANESPFDNEY RTNFARLNRY SDCQPKALIA
     AYAAYAGVKP EQTLTSRGAD EGIELLIRAF CETNEDAILY CPPTYGMYSV SAETIGVERK
     TVPLTEDWQL DLSGIEANLD KVKLVFVCSP NNPTGNLVKR EDIIALLEMT KDRAIVVMDE
     AYIDFCPEAS TVDLLAQYSN LAILRTLSKA FALAGLRCGF TLANEELINV LLKVIAPYPV
     PVPVAEIATQ ALSEAGLARA KFQVLDLNAN RAYLQVGLSM IAGLEVFEGW GNYLLVKFPN
     GDELFKAAWE SGIILRNSPI KDCVRISVGS RDECEKTLGF IRNYYS