ID   HIS8_LACLA              Reviewed;         360 AA.
AC   Q02135; O34130;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 3.
DT   25-MAY-2022, entry version 135.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
GN   Name=hisC; OrderedLocusNames=LL1206; ORFNames=L0065;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCDO 2118;
RX   PubMed=1400209; DOI=10.1128/jb.174.20.6571-6579.1992;
RA   Delorme C., Ehrlich S.D., Renault P.;
RT   "Histidine biosynthesis genes in Lactococcus lactis subsp. lactis.";
RL   J. Bacteriol. 174:6571-6579(1992).
RN   [2]
RP   SEQUENCE REVISION.
RA   Delorme C., Goupil-Feuillerat N., Godon J.-J., Ehrlich S.D., Renault P.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; U92974; AAB81901.1; -; Genomic_DNA.
DR   EMBL; AE005176; AAK05304.1; -; Genomic_DNA.
DR   PIR; B45734; B45734.
DR   PIR; F86775; F86775.
DR   RefSeq; NP_267362.1; NC_002662.1.
DR   RefSeq; WP_010905826.1; NC_002662.1.
DR   AlphaFoldDB; Q02135; -.
DR   SMR; Q02135; -.
DR   STRING; 272623.L0065; -.
DR   PaxDb; Q02135; -.
DR   EnsemblBacteria; AAK05304; AAK05304; L0065.
DR   KEGG; lla:L0065; -.
DR   PATRIC; fig|272623.7.peg.1301; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_0_9; -.
DR   OMA; FDGYPIL; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000002196; 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..360
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153376"
FT   MOD_RES         208
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        24
FT                   /note="I -> M (in Ref. 2; AAB81901)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="D -> E (in Ref. 2; AAB81901)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        79
FT                   /note="I -> F (in Ref. 2; AAB81901)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        135
FT                   /note="L -> S (in Ref. 2; AAB81901)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="D -> N (in Ref. 2; AAB81901)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        179
FT                   /note="N -> D (in Ref. 2; AAB81901)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        304
FT                   /note="E -> D (in Ref. 2; AAB81901)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   360 AA;  41401 MW;  C747B7E8C3495AC1 CRC64;
     MSWQNNLRSV SPYIAGEQPE LTDIIKLNTN ENPYPPTSVA QLFNERYKTK NLRLYPSTDA
     KSLRKKLADY HHLEVEQVII GNGSDEVLSL SFLTFFNSQS PLLMPDITYS FYPIYCELYR
     IPFQKVPVDD DFKVLIKDYC IENGGIVIAN PDAPTALALN LKDIEEILKK NQNSIVLINE
     AYIDFGGETC LPLLKKYDNL VVVQTFSKSR SLAGIRLGVA YGSAEAISHL YDVKNSFNSY
     PIDSLAQIIG EASLMDEHYF QKNIQKIIKT REVFKDNLVN LGFEVTDSKA NFVFVHHPKV
     KAEELFKALY EAKIIVRHWN QPRIDDWLRI TIGTNKEMNK VIEFLKGYLK KNEEIDEWKK