ID   HIS8_ECOLI              Reviewed;         356 AA.
AC   P06986;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   02-SEP-2026, entry version 207.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
DE            Short=HPAT;
DE            Short=HspAT;
GN   Name=hisC; OrderedLocusNames=b2021, JW2003;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=3062174; DOI=10.1016/0022-2836(88)90194-5;
RA   Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.;
RT   "Structure and function of the Salmonella typhimurium and Escherichia coli
RT   K-12 histidine operons.";
RL   J. Mol. Biol. 203:585-606(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=K12;
RX   PubMed=2999081; DOI=10.1128/jb.164.3.1317-1323.1985;
RA   Grisolia V., Carlomagno M.S., Nappo A.G., Bruni C.B.;
RT   "Cloning, structure, and expression of the Escherichia coli K-12 hisC
RT   gene.";
RL   J. Bacteriol. 164:1317-1323(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RC   STRAIN=K12;
RX   PubMed=8201624; DOI=10.1006/jmbi.1994.1384;
RA   Jovanovic G., Kostic T., Jankovic M., Savic D.J.;
RT   "Nucleotide sequence of the Escherichia coli K12 histidine operon
RT   revisited.";
RL   J. Mol. Biol. 239:433-435(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), COFACTOR, AND SUBUNIT.
RX   PubMed=11518529; DOI=10.1006/jmbi.2001.4882;
RA   Sivaraman J., Li Y., Larocque R., Schrag J.D., Cygler M., Matte A.;
RT   "Crystal structure of histidinol phosphate aminotransferase (HisC) from
RT   Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and
RT   L-histidinol phosphate.";
RL   J. Mol. Biol. 311:761-776(2001).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-351 IN COMPLEX WITH PYRIDOXAL
RP   5'-PHOSPHATE; HISTIDINOL-PHOSPHATE AND N-(5'-PHOSPHOPYRIDOXYL)-L-GLUTAMATE,
RP   AND COFACTOR.
RX   PubMed=11294630; DOI=10.1021/bi002769u;
RA   Haruyama K., Nakai T., Miyahara I., Hirotsu K., Mizuguchi H., Hayashi H.,
RA   Kagamiyama H.;
RT   "Structures of Escherichia coli histidinol-phosphate aminotransferase and
RT   its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-
RT   glutamate: double substrate recognition of the enzyme.";
RL   Biochemistry 40:4633-4644(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidinol phosphate + 2-oxoglutarate = 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:0000269|PubMed:2999081};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:11294630, ECO:0000269|PubMed:11518529};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC       {ECO:0000269|PubMed:2999081}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11294630,
CC       ECO:0000269|PubMed:11518529}.
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; X03416; CAA27150.1; -; Genomic_DNA.
DR   EMBL; X13462; CAA31813.1; -; Genomic_DNA.
DR   EMBL; U02071; AAA19743.1; -; Unassigned_DNA.
DR   EMBL; U00096; AAC75082.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15852.1; -; Genomic_DNA.
DR   PIR; D64967; XNECHC.
DR   RefSeq; NP_416525.1; NC_000913.3.
DR   RefSeq; WP_000108941.1; NZ_CP009789.1.
DR   PDB; 1FG3; X-ray; 2.20 A; A=1-356.
DR   PDB; 1FG7; X-ray; 1.50 A; A=1-356.
DR   PDB; 1GEW; X-ray; 2.00 A; A=1-356.
DR   PDB; 1GEX; X-ray; 2.20 A; A=1-356.
DR   PDB; 1GEY; X-ray; 2.30 A; A=1-356.
DR   PDB; 1IJI; X-ray; 2.20 A; A=1-356.
DR   AlphaFoldDB; P06986; -.
DR   SMR; P06986; -.
DR   BioGRID; 4260404; 29.
DR   DIP; DIP-9902N; -.
DR   FunCoup; P06986; 693.
DR   IntAct; P06986; 5.
DR   STRING; 511145.b2021; -.
DR   DrugBank; DB03997; L-histidinol phosphate.
DR   DrugBank; DB02142; Pyridoxamine-5'-Phosphate.
DR   DrugBank; DB01813; Pyridoxyl-Glutamic Acid-5'-Monophosphate.
DR   jPOST; P06986; -.
DR   PaxDb; 511145-b2021; -.
DR   EnsemblBacteria; AAC75082; AAC75082; b2021.
DR   GeneID; 946551; -.
DR   KEGG; ecj:JW2003; -.
DR   KEGG; eco:b2021; -.
DR   KEGG; ecoc:C3026_11395; -.
DR   PATRIC; fig|1411691.4.peg.231; -.
DR   EchoBASE; EB0441; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_1_6; -.
DR   InParanoid; P06986; -.
DR   OMA; NFVQFGR; -.
DR   OrthoDB; 9813612at2; -.
DR   PhylomeDB; P06986; -.
DR   BioCyc; EcoCyc:HISTPHOSTRANS-MONOMER; -.
DR   BioCyc; MetaCyc:HISTPHOSTRANS-MONOMER; -.
DR   BRENDA; 2.6.1.9; 2026.
DR   UniPathway; UPA00031; UER00012.
DR   EvolutionaryTrace; P06986; -.
DR   PRO; PR:P06986; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0004400; F:L-histidinol-phosphate:2-oxoglutarate transaminase activity; IDA:EcoCyc.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:L-histidine biosynthetic process; IMP:EcoCyc.
DR   CDD; cd00609; AAT_like; 1.
DR   FunFam; 3.40.640.10:FF:000032; Histidinol-phosphate aminotransferase; 1.
DR   FunFam; 3.90.1150.10:FF:000042; Histidinol-phosphate aminotransferase; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II_large.
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   NCBIfam; TIGR01141; hisC; 1.
DR   PANTHER; PTHR42885:SF2; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
DR   PDBsum; 1FG3; -.
DR   PDBsum; 1FG7; -.
DR   PDBsum; 1GEW; -.
DR   PDBsum; 1GEX; -.
DR   PDBsum; 1GEY; -.
DR   PDBsum; 1IJI; -.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Aminotransferase;
KW   Histidine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..356
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153360"
FT   MOD_RES         214
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   CONFLICT        130
FT                   /note="L -> P (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149
FT                   /note="V -> A (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   HELIX           6..9
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           12..16
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   TURN            27..29
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:1GEW"
FT   HELIX           55..57
FT                   /evidence="ECO:0007829|PDB:1GEW"
FT   HELIX           61..71
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           83..95
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   TURN            98..100
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   STRAND          102..105
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           112..120
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   STRAND          123..126
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           137..141
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   STRAND          147..155
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   TURN            157..159
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           161..164
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           165..175
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   TURN            176..178
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   STRAND          180..184
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           188..190
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           192..194
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           197..199
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   TURN            200..202
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   STRAND          206..214
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   STRAND          224..228
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           230..239
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           247..256
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           259..285
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   STRAND          289..292
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   STRAND          296..304
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           307..316
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   STRAND          333..337
FT                   /evidence="ECO:0007829|PDB:1FG7"
FT   HELIX           341..352
FT                   /evidence="ECO:0007829|PDB:1FG7"
SQ   SEQUENCE   356 AA;  39360 MW;  056CBB3CF894083F CRC64;
     MSTVTITDLA RENVRNLTPY QSARRLGGNG DVWLNANEYP TAVEFQLTQQ TLNRYPECQP
     KAVIENYAQY AGVKPEQVLV SRGADEGIEL LIRAFCEPGK DAILYCPPTY GMYSVSAETI
     GVECRTVPTL DNWQLDLQGI SDKLDGVKVV YVCSPNNPTG QLINPQDFRT LLELTRGKAI
     VVADEAYIEF CPQASLAGWL AEYPHLAILR TLSKAFALAG LRCGFTLANE EVINLLMKVI
     APYPLSTPVA DIAAQALSPQ GIVAMRERVA QIIAEREYLI AALKEIPCVE QVFDSETNYI
     LARFKASSAV FKSLWDQGII LRDQNKQPSL SGCLRITVGT REESQRVIDA LRAEQV
//