HIS82_CUPPJ
ID HIS82_CUPPJ Reviewed; 366 AA.
AC Q46WL3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Histidinol-phosphate aminotransferase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01023};
GN Name=hisC2 {ECO:0000255|HAMAP-Rule:MF_01023}; OrderedLocusNames=Reut_A3110;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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 -!- 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 -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01023}.
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DR EMBL; CP000090; AAZ62470.1; -; Genomic_DNA.
DR RefSeq; WP_011299253.1; NC_007347.1.
DR PDB; 3EUC; X-ray; 2.05 A; A/B=1-366.
DR PDBsum; 3EUC; -.
DR AlphaFoldDB; Q46WL3; -.
DR SMR; Q46WL3; -.
DR STRING; 264198.Reut_A3110; -.
DR DNASU; 3609701; -.
DR EnsemblBacteria; AAZ62470; AAZ62470; Reut_A3110.
DR KEGG; reu:Reut_A3110; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_1_4; -.
DR OMA; IWLNANE; -.
DR OrthoDB; 1248286at2; -.
DR UniPathway; UPA00031; UER00012.
DR EvolutionaryTrace; Q46WL3; -.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase;
KW Histidine biosynthesis; Pyridoxal phosphate; Transferase.
FT CHAIN 1..366
FT /note="Histidinol-phosphate aminotransferase 2"
FT /id="PRO_0000153429"
FT MOD_RES 226
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 15..19
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 68..79
FT /evidence="ECO:0007829|PDB:3EUC"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:3EUC"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:3EUC"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:3EUC"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:3EUC"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:3EUC"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:3EUC"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:3EUC"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 209..213
FT /evidence="ECO:0007829|PDB:3EUC"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:3EUC"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 258..268
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 271..293
FT /evidence="ECO:0007829|PDB:3EUC"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 315..323
FT /evidence="ECO:0007829|PDB:3EUC"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:3EUC"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:3EUC"
FT HELIX 350..363
FT /evidence="ECO:0007829|PDB:3EUC"
SQ SEQUENCE 366 AA; 39607 MW; D979A3B063F852E6 CRC64;
MSVVDPSLIE RIIRDDVRAM GAYHVPDSHG LVKLDAMENP YRLPPALRSE LAARLGEVAL
NRYPVPSSEA LRAKLKEVMQ VPAGMEVLLG NGSDEIISML ALAAARPGAK VMAPVPGFVM
YAMSAQFAGL EFVGVPLRAD FTLDRGAMLA AMAEHQPAIV YLAYPNNPTG NLFDAADMEA
IVRAAQGSVC RSLVVVDEAY QPFAQESWMS RLTDFGNLLV MRTVSKLGLA GIRLGYVAGD
PQWLEQLDKV RPPYNVNVLT EATALFALEH VAVLDEQAAQ LRAERSRVAE GMAAHGGVTV
FPSAANFLLA RVPDAAQTFD RLLARKVLIK NVSKMHPLLA NCLRVTVSTP EENAQFLEAF
AASLQD
