HIS8_ECOLI
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 03-AUG-2022, entry version 192.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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=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: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_SSTT01000011.1.
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 PDBsum; 1FG3; -.
DR PDBsum; 1FG7; -.
DR PDBsum; 1GEW; -.
DR PDBsum; 1GEX; -.
DR PDBsum; 1GEY; -.
DR PDBsum; 1IJI; -.
DR AlphaFoldDB; P06986; -.
DR SMR; P06986; -.
DR BioGRID; 4260404; 25.
DR DIP; DIP-9902N; -.
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; P06986; -.
DR PRIDE; P06986; -.
DR EnsemblBacteria; AAC75082; AAC75082; b2021.
DR EnsemblBacteria; BAA15852; BAA15852; BAA15852.
DR GeneID; 946551; -.
DR KEGG; ecj:JW2003; -.
DR KEGG; eco:b2021; -.
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; IWLNANE; -.
DR PhylomeDB; P06986; -.
DR BioCyc; EcoCyc:HISTPHOSTRANS-MON; -.
DR BioCyc; MetaCyc:HISTPHOSTRANS-MON; -.
DR BRENDA; 2.6.1.9; 2026.
DR UniPathway; UPA00031; UER00012.
DR EvolutionaryTrace; P06986; -.
DR PRO; PR:P06986; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IMP:EcoCyc.
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 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 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 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
