ID   HIS8_SYNE7              Reviewed;         373 AA.
AC   Q31PF9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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};
GN   OrderedLocusNames=Synpcc7942_1030;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) 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; CP000100; ABB57060.1; -; Genomic_DNA.
DR   RefSeq; WP_011377834.1; NC_007604.1.
DR   AlphaFoldDB; Q31PF9; -.
DR   SMR; Q31PF9; -.
DR   STRING; 1140.Synpcc7942_1030; -.
DR   PRIDE; Q31PF9; -.
DR   DNASU; 3773960; -.
DR   EnsemblBacteria; ABB57060; ABB57060; Synpcc7942_1030.
DR   KEGG; syf:Synpcc7942_1030; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_1_3; -.
DR   OMA; YPDMACT; -.
DR   OrthoDB; 1248286at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1030-MON; -.
DR   UniPathway; UPA00031; UER00012.
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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..373
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_1000063507"
FT   MOD_RES         230
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   373 AA;  40659 MW;  D5874FB4CB1A79D5 CRC64;
     MLPFLRSELA RCQPYHPNPG GTGMAMDILD TNECPYDLPT DLKQTLADRY VEAIASNRYP
     DGSHTDLKAA IVDYLSEQTA GQWQPGPEHV TVGNGSDELI RSILIATCLG GQGSVLVAEP
     TFSMYGIVAE TLGIPVVRIG RDPQTWEMDL AAAETAITQT EGTPVRLCFV VHPNSPTANP
     LTEAEKDWLR QVPPQILVVI DEAYFEFSGE TLLAELPQHP NWLITRTFSK ALRLAAHRVG
     YGIGDPQLIA ALEAIRLPYN LPSVAQLAAT LALEARSQLL SAIPRLITER DRLYRKLQVV
     SQLQVWPSAS NFLFLKTQSS SQTAALAAQL KAQGTLVRHT ADGLRITIGS PAENERTLAH
     LQTAITQSLP ATV