ID   HIS81_OCEIH             Reviewed;         354 AA.
AC   Q8ESS3;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 109.
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=OB0545;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(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;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       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; BA000028; BAC12501.1; -; Genomic_DNA.
DR   RefSeq; WP_011064948.1; NC_004193.1.
DR   AlphaFoldDB; Q8ESS3; -.
DR   SMR; Q8ESS3; -.
DR   STRING; 221109.22776224; -.
DR   EnsemblBacteria; BAC12501; BAC12501; BAC12501.
DR   KEGG; oih:OB0545; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_0_9; -.
DR   OMA; FDGYPIL; -.
DR   OrthoDB; 1248286at2; -.
DR   PhylomeDB; Q8ESS3; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000000822; 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..354
FT                   /note="Histidinol-phosphate aminotransferase 1"
FT                   /id="PRO_0000153407"
FT   MOD_RES         209
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  40160 MW;  C01145BE489C966D CRC64;
     MSKFWSSLAK QVDPYIPGEQ LNDDTIIKLN TNENPYPPSN QVIQAIDEAS KNLRLYPSPT
     VDELRSEIGE MYGLSQDHIF IGNGSDEVLA FSFMSFFEPG NRIKYPEITY SFYPVYAKLF
     NISTDVIPLN DDYTIPVEHF YNSEGGVIFP NPNAPTGIFL EIDQIKRILE NNPNQVVIID
     EAYIDFALES AVTLVEAFPN LLVIQTMSKS RSLAGLRIGF AIGNPELIIG LERIKNSFNS
     YTVDRLAIAG AIEAIRDKDY FLQTTTKIIE SRSYLKEQLE TRHFDILPSQ ANFLLVSHKE
     VNAEVLYQEL KKQGILVRYF QKPGLENFLR ISIGTPAQIE KLLKKIDHII KPSP