HIS8_PARDP
ID HIS8_PARDP Reviewed; 367 AA.
AC Q51687; A1B1W6;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 25-MAY-2022, entry version 121.
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}; Synonyms=hisH;
GN OrderedLocusNames=Pden_1409;
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9043133; DOI=10.1099/00221287-143-2-563;
RA Page D., Pearce D.A., Norris H.A., Ferguson S.J.;
RT "The Paracoccus denitrificans ccmA, B and C genes: cloning and sequencing,
RT and analysis of the potential of their products to form a haem or apo-c-
RT type cytochrome transporter.";
RL Microbiology 143:563-576(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; Z71971; CAA96498.1; -; Genomic_DNA.
DR EMBL; CP000489; ABL69510.1; -; Genomic_DNA.
DR RefSeq; WP_011747728.1; NC_008686.1.
DR AlphaFoldDB; Q51687; -.
DR SMR; Q51687; -.
DR STRING; 318586.Pden_1409; -.
DR PRIDE; Q51687; -.
DR EnsemblBacteria; ABL69510; ABL69510; Pden_1409.
DR KEGG; pde:Pden_1409; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_3_5; -.
DR OMA; YPDMACT; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000000361; Chromosome 1.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..367
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_0000153409"
FT MOD_RES 221
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
FT CONFLICT 9
FT /note="A -> R (in Ref. 1; CAA96498)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="Missing (in Ref. 1; CAA96498)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="N -> K (in Ref. 1; CAA96498)"
FT /evidence="ECO:0000305"
FT CONFLICT 185..186
FT /note="AI -> RIA (in Ref. 1; CAA96498)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="E -> Q (in Ref. 1; CAA96498)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..209
FT /note="TR -> QA (in Ref. 1; CAA96498)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="G -> A (in Ref. 1; CAA96498)"
FT /evidence="ECO:0000305"
FT CONFLICT 357..363
FT /note="GQYMAER -> ASTWPSA (in Ref. 1; CAA96498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 39582 MW; 49C86EA0501EB76B CRC64;
MSQNQTTIAP QPGIMEISLY EGGASKVAGV ENVVKLSSNE NPFGPSDKAR EAMIRAAHGL
HRYPNTDHAG LRGAIGEVHG LDPDRIICGV GSDEIIHFLC QAYAGPGTEV LFTEHGFLMY
RISAHAAGAI PVQVAERDRV TDIDALIAGA TPRTRLIFVA NPNNPTGTMV GLPELERLAR
AVPQAILVVD AAYAEYVGDY DGGAELATRL PNVFMTRTFS KIYGLGGLRV GWGYGPREIV
DVLNRIRGPF NLSNVALEGA EAAMRDREHI ARCQAENARM RAWLAEALAE KGVPSDTSCA
NFILARFADA ETAGACDEYL KTQGLIVRRV AGYGLPHCLR ITIGDEASCR RVAHVIGQYM
AERAESR
