HIS8_THEMA
ID HIS8_THEMA Reviewed; 335 AA.
AC Q9X0D0;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 143.
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}; OrderedLocusNames=TM_1040;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 6-335, COFACTOR, SUBUNIT, AND
RP N6-(PYRIDOXAL PHOSPHATE)LYSINE.
RX PubMed=15007066; DOI=10.1074/jbc.m400291200;
RA Fernandez F.J., Vega M.C., Lehmann F., Sandmeier E., Gehring H.,
RA Christen P., Wilmanns M.;
RT "Structural studies of the catalytic reaction pathway of a
RT hyperthermophilic histidinol-phosphate aminotransferase.";
RL J. Biol. Chem. 279:21478-21488(2004).
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 ECO:0000269|PubMed:15007066};
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 ECO:0000269|PubMed:15007066}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01023}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000512; AAD36117.1; -; Genomic_DNA.
DR PIR; G72304; G72304.
DR RefSeq; NP_228846.1; NC_000853.1.
DR RefSeq; WP_004080482.1; NZ_CP011107.1.
DR PDB; 1H1C; X-ray; 2.85 A; A/B/C/D=1-335.
DR PDB; 1UU0; X-ray; 2.85 A; A/B/C/D=1-335.
DR PDB; 1UU1; X-ray; 2.38 A; A/B/C/D=1-335.
DR PDB; 1UU2; X-ray; 2.80 A; A/B=1-335.
DR PDB; 2F8J; X-ray; 2.40 A; A/B/C/D=1-335.
DR PDBsum; 1H1C; -.
DR PDBsum; 1UU0; -.
DR PDBsum; 1UU1; -.
DR PDBsum; 1UU2; -.
DR PDBsum; 2F8J; -.
DR AlphaFoldDB; Q9X0D0; -.
DR SMR; Q9X0D0; -.
DR STRING; 243274.THEMA_09160; -.
DR DrugBank; DB03997; L-histidinol phosphate.
DR DrugBank; DB02142; Pyridoxamine-5'-Phosphate.
DR DNASU; 897350; -.
DR EnsemblBacteria; AAD36117; AAD36117; TM_1040.
DR KEGG; tma:TM1040; -.
DR eggNOG; COG0079; Bacteria.
DR InParanoid; Q9X0D0; -.
DR OMA; IWLNANE; -.
DR OrthoDB; 1248286at2; -.
DR BRENDA; 2.6.1.9; 6331.
DR SABIO-RK; Q9X0D0; -.
DR UniPathway; UPA00031; UER00012.
DR EvolutionaryTrace; Q9X0D0; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0000105; P:histidine biosynthetic process; IDA:UniProtKB.
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..335
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_0000153470"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:15007066,
FT ECO:0007744|PDB:1H1C"
FT HELIX 2..5
FT /evidence="ECO:0007829|PDB:1UU1"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1UU1"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:1UU1"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:1UU1"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:1UU1"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1UU1"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1UU1"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:1UU1"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:1UU1"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1UU1"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:1UU1"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:1UU1"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:1UU1"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:1UU1"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:1UU1"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1UU1"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:1UU1"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:1UU1"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:1UU1"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:1UU1"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:1UU1"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1UU1"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:1UU1"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:1UU1"
FT HELIX 248..272
FT /evidence="ECO:0007829|PDB:1UU1"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:1UU1"
FT HELIX 291..302
FT /evidence="ECO:0007829|PDB:1UU1"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:1UU1"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:1UU1"
FT HELIX 321..332
FT /evidence="ECO:0007829|PDB:1UU1"
SQ SEQUENCE 335 AA; 39298 MW; D7CA1B807825376A CRC64;
MNPLDLIAKR AYPYETEKRD KTYLALNENP FPFPEDLVDE VFRRLNSDAL RIYYDSPDEE
LIEKILSYLD TDFLSKNNVS VGNGADEIIY VMMLMFDRSV FFPPTYSCYR IFAKAVGAKF
LEVPLTKDLR IPEVNVGEGD VVFIPNPNNP TGHVFEREEI ERILKTGAFV ALDEAYYEFH
GESYVDFLKK YENLAVIRTF SKAFSLAAQR VGYVVASEKF IDAYNRVRLP FNVSYVSQMF
AKVALDHREI FEERTKFIVE ERERMKSALR EMGYRITDSR GNFVFVFMEK EEKERLLEHL
RTKNVAVRSF REGVRITIGK REENDMILRE LEVFK
