HIS8_YEAST
ID HIS8_YEAST Reviewed; 385 AA.
AC P07172; D6VVH1;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000305};
DE EC=2.6.1.9 {ECO:0000305|PubMed:14190241};
DE AltName: Full=Imidazole acetol-phosphate transaminase;
GN Name=HIS5 {ECO:0000303|Ref.4}; OrderedLocusNames=YIL116W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3302607; DOI=10.1007/bf00330437;
RA Nishiwaki K., Hayashi N., Irie S., Chung D.-H., Harashima S., Oshima Y.;
RT "Structure of the yeast HIS5 gene responsive to general control of amino
RT acid biosynthesis.";
RL Mol. Gen. Genet. 208:159-167(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RA Chung D.H., Nishiwaki K., Oshima Y.;
RT "Studies on the HIS5 gene of yeast: the nucleotide sequence of 5' upstream
RT region of the HIS5 gene of Saccharomyces cerevisiae.";
RL Sanop Misaengmul Hakhoe Chi 13:19-25(1985).
RN [5]
RP CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=14190241; DOI=10.1126/science.146.3643.525;
RA Fink G.R.;
RT "Gene-enzyme relations in histidine biosynthesis in yeast.";
RL Science 146:525-527(1964).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29897761; DOI=10.1021/acs.jproteome.8b00032;
RA He C., Jia C., Zhang Y., Xu P.;
RT "Enrichment-based proteogenomics identifies microproteins, missing
RT proteins, and novel smORFs in Saccharomyces cerevisiae.";
RL J. Proteome Res. 17:2335-2344(2018).
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;
CC Evidence={ECO:0000305|PubMed:14190241};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC {ECO:0000305|PubMed:14190241}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; Z38125; CAA86264.1; -; Genomic_DNA.
DR EMBL; X05650; CAA29139.1; -; Genomic_DNA.
DR EMBL; M38613; AAA34675.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08437.1; -; Genomic_DNA.
DR PIR; S48456; S48456.
DR RefSeq; NP_012150.1; NM_001179464.1.
DR AlphaFoldDB; P07172; -.
DR SMR; P07172; -.
DR BioGRID; 34875; 19.
DR STRING; 4932.YIL116W; -.
DR iPTMnet; P07172; -.
DR MaxQB; P07172; -.
DR PaxDb; P07172; -.
DR PRIDE; P07172; -.
DR TopDownProteomics; P07172; -.
DR EnsemblFungi; YIL116W_mRNA; YIL116W; YIL116W.
DR GeneID; 854690; -.
DR KEGG; sce:YIL116W; -.
DR SGD; S000001378; HIS5.
DR VEuPathDB; FungiDB:YIL116W; -.
DR eggNOG; KOG0633; Eukaryota.
DR HOGENOM; CLU_017584_3_1_1; -.
DR InParanoid; P07172; -.
DR OMA; IWLNANE; -.
DR BioCyc; YEAST:YIL116W-MON; -.
DR UniPathway; UPA00031; UER00012.
DR PRO; PR:P07172; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P07172; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IMP:SGD.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IMP:SGD.
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 Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..385
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_0000153509"
FT MOD_RES 230
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000305"
FT CONFLICT 110..112
FT /note="PGK -> RE (in Ref. 1; CAA29139)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="Y -> S (in Ref. 1; CAA29139)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="T -> I (in Ref. 1; CAA29139)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="R -> L (in Ref. 1; CAA29139)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 42646 MW; E026E09DB0443C45 CRC64;
MVFDLKRIVR PKIYNLEPYR CARDDFTEGI LLDANENAHG PTPVELSKTN LHRYPDPHQL
EFKTAMTKYR NKTSSYANDP EVKPLTADNL CLGVGSDESI DAIIRACCVP GKEKILVLPP
TYSMYSVCAN INDIEVVQCP LTVSDGSFQM DTEAVLTILK NDSLIKLMFV TSPGNPTGAK
IKTSLIEKVL QNWDNGLVVV DEAYVDFCGG STAPLVTKYP NLVTLQTLSK SFGLAGIRLG
MTYATAELAR ILNAMKAPYN ISSLASEYAL KAVQDSNLKK MEATSKIINE EKMRLLKELT
ALDYVDDQYV GGLDANFLLI RINGGDNVLA KKLYYQLATQ SGVVVRFRGN ELGCSGCLRI
TVGTHEENTH LIKYFKETLY KLANE
