HIS8_ZYMMO
ID HIS8_ZYMMO Reviewed; 369 AA.
AC P34037; Q5NQF9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 3.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01023};
DE EC=2.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01023, ECO:0000269|PubMed:7883715};
DE AltName: Full=Imidazole acetol phosphate aminotransferase {ECO:0000303|PubMed:7883715};
DE Short=IAP aminotransferase {ECO:0000303|PubMed:7883715};
DE AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000255|HAMAP-Rule:MF_01023};
GN Name=hisC {ECO:0000255|HAMAP-Rule:MF_01023};
GN Synonyms=hisH {ECO:0000303|PubMed:7883715}; OrderedLocusNames=ZMO0421;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=7883715; DOI=10.1128/jb.177.6.1576-1584.1995;
RA Gu W., Zhao G.S., Eddy C., Jensen R.A.;
RT "Imidazole acetol phosphate aminotransferase in Zymomonas mobilis:
RT molecular genetic, biochemical, and evolutionary analyses.";
RL J. Bacteriol. 177:1576-1584(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 192-369.
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=7916685; DOI=10.1111/j.1432-1033.1993.tb17646.x;
RA Zhao G., Xia T., Ingram L.O., Jensen R.A.;
RT "An allosterically insensitive class of cyclohexadienyl dehydrogenase from
RT Zymomonas mobilis.";
RL Eur. J. Biochem. 212:157-165(1993).
CC -!- FUNCTION: Catalyzes the conversion of imidazole acetol phosphate to
CC histidinol phosphate. Can also transaminate aromatic amino acids and
CC histidine in addition to histidinol phosphate.
CC {ECO:0000269|PubMed:7883715}.
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, ECO:0000269|PubMed:7883715};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01023,
CC ECO:0000269|PubMed:7883715};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.17 mM for histidinol phosphate {ECO:0000269|PubMed:7883715};
CC KM=3.39 mM for tyrosine {ECO:0000269|PubMed:7883715};
CC KM=43.48 mM for phenylalanine {ECO:0000269|PubMed:7883715};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:7883715};
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:7883715}.
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; L36343; AAC41445.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV89045.1; -; Genomic_DNA.
DR EMBL; X67208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S29383; S29383.
DR RefSeq; WP_011240336.1; NZ_CP035711.1.
DR AlphaFoldDB; P34037; -.
DR SMR; P34037; -.
DR STRING; 264203.ZMO0421; -.
DR EnsemblBacteria; AAV89045; AAV89045; ZMO0421.
DR GeneID; 58026265; -.
DR KEGG; zmo:ZMO0421; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_3_5; -.
DR OMA; YPDMACT; -.
DR OrthoDB; 1248286at2; -.
DR SABIO-RK; P34037; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000001173; Chromosome.
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 Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..369
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_0000153489"
FT MOD_RES 223
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
FT CONFLICT 279..286
FT /note="NKKWRGWF -> SKKVAWLV (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="A -> V (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="E -> K (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 40342 MW; D9736E098A8FF05D CRC64;
MTAAPELRPK SWIDSIAPYI PGSSKTLDGR PAVKLSSNEN PLGTSLKAKE AYREAIDSLS
LYPDSGATAL REAIGACYNL DPARIIHGTG SDEILHLAAG AYAGQDDEVL YPRYSFSVYP
LAARRVGATP VEAPDDDYRC SVDALLKAVT PRTRVVFIAN PNNPTGTWIT RAEVEKLHNG
LPRNCLLVID QAYAEYLDPE CDDGALALAK NTKNVLVTRT FSKIYGLAAE RIGWAYACPE
IIDALNRIRA PFNVTIAGQK AAVAALEDQA FIQNSFKHNK KWRGWFENQM ALLSNAGIRV
IPSSANFTLL LFEGSLTAET AYKALMDHGY TTRWLPGQRL PHALRITIGS EKHMQDVAGI
LTSLVRQAL
