ID   HIS8_STRCO              Reviewed;         369 AA.
AC   P16246;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 142.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
GN   Name=hisC; OrderedLocusNames=SCO2053; ORFNames=SC4G6.22c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=2199329; DOI=10.1016/0378-1119(90)90436-u;
RA   Limauro D., Avitabile A., Cappellano M., Puglia A.M., Bruni C.B.;
RT   "Cloning and characterization of the histidine biosynthetic gene cluster of
RT   Streptomyces coelicolor A3(2).";
RL   Gene 90:31-41(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(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; M31628; AAA26756.1; -; Genomic_DNA.
DR   EMBL; AL939111; CAB51445.1; -; Genomic_DNA.
DR   PIR; JQ0637; JQ0637.
DR   RefSeq; NP_626313.1; NC_003888.3.
DR   RefSeq; WP_003976762.1; NZ_VNID01000001.1.
DR   AlphaFoldDB; P16246; -.
DR   SMR; P16246; -.
DR   STRING; 100226.SCO2053; -.
DR   PRIDE; P16246; -.
DR   GeneID; 1097487; -.
DR   KEGG; sco:SCO2053; -.
DR   PATRIC; fig|100226.15.peg.2085; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_1_11; -.
DR   InParanoid; P16246; -.
DR   OMA; IWLNANE; -.
DR   PhylomeDB; P16246; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000001973; 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..369
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153463"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         230
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   369 AA;  40388 MW;  AA572A9BB0C93E08 CRC64;
     MTFGIDDLPV RDELRGKSPY GAPQLDVPVR LNTNENPYPL PEALVERIAE RVREAARDLN
     RYPDRDAVEL RTQLARYLTD TSGHPLDVSN VWAANGSNEV IQQLLQTFGG PGRTAIGFEP
     SYSMHGLIAR GTGTGWISGP RHEDFTIDVP AATRAIDEHR PDVVFITTPN NPTGTAVPAE
     TVLALYEAAQ AAKPSMVVVD EAYIEFSHGA SLLPLLDGRP NLVVSRTMSK AFGAAGLRLG
     YLAAHPAVVD AVQLVRLPYH LSAVTQATAL AALEHTDTLL KYVEQLKTER DRLVAELRAI
     GYAVTESDAN FVQFGRFADS HATWRKILDR GVLVRDNGVP GWLRVTAGTP EENDAFLDAV
     REVKKEQHT