ID   HIS8_SYNY3              Reviewed;         349 AA.
AC   P73807;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 2.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
GN   Name=hisC; OrderedLocusNames=sll1958;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA17861.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000022; BAA17861.1; ALT_INIT; Genomic_DNA.
DR   PIR; S74900; S74900.
DR   AlphaFoldDB; P73807; -.
DR   SMR; P73807; -.
DR   STRING; 1148.1652943; -.
DR   PaxDb; P73807; -.
DR   EnsemblBacteria; BAA17861; BAA17861; BAA17861.
DR   KEGG; syn:sll1958; -.
DR   eggNOG; COG0079; Bacteria.
DR   InParanoid; P73807; -.
DR   OMA; IWLNANE; -.
DR   PhylomeDB; P73807; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000001425; 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..349
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153467"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         207
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   349 AA;  38702 MW;  239C3F26DCF4F2C6 CRC64;
     MVSIRPSVRH TPAYVPGEQP QTNDFIKLNT NENPYDPPAQ VLAAVAAELP KVRLYPDPVS
     TQLRQAAADL YGVDLNQVLA GNGSDDILNI VVRTFVDPGE TVAFLDLTYS LYETIASVHG
     AKVQKIATDA NFDLTGPVIC PEAKLIFLAS PNPPKGKHLN REFLWQTCAQ AEGVVVIDEA
     YGDFSDEDHW DFLQEFDNVI ISRTLSKSYS LAGMRVGLAI AAPALIEEMD KVRDSYNLDR
     LAQVLGTAAL RNQAEFVPLW EKVRHTRTRL MEQLAELDFQ VCPSDANFVF AAPRWMAAAD
     LYQALKEKKI LVRYFNHPRI TDYLRITVGT DGEIDQLLLA IASLKGSLG