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HIS8_SCHPO
ID   HIS8_SCHPO              Reviewed;         384 AA.
AC   P36605;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 149.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
GN   Name=his3; ORFNames=pi009, SPBC11B10.02c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=8159167; DOI=10.1007/bf00391010;
RA   Burke J.D., Gould K.L.;
RT   "Molecular cloning and characterization of the Schizosaccharomyces pombe
RT   his3 gene for use as a selectable marker.";
RL   Mol. Gen. Genet. 242:169-176(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10620777;
RX   DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA   Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA   Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA   Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT   "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT   yeast chromosome II: sequence analysis and characterization of the genomic
RT   DNA and cDNAs encoded on the segment.";
RL   Yeast 16:71-80(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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   -!- 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   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; L19523; AAA67316.1; -; Genomic_DNA.
DR   EMBL; L19524; AAA86664.1; -; Genomic_DNA.
DR   EMBL; AB004534; BAA21386.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAC37506.1; -; Genomic_DNA.
DR   PIR; S41584; S41584.
DR   RefSeq; NP_595622.1; NM_001021516.2.
DR   AlphaFoldDB; P36605; -.
DR   SMR; P36605; -.
DR   BioGRID; 276251; 4.
DR   STRING; 4896.SPBC11B10.02c.1; -.
DR   iPTMnet; P36605; -.
DR   MaxQB; P36605; -.
DR   PaxDb; P36605; -.
DR   PRIDE; P36605; -.
DR   EnsemblFungi; SPBC11B10.02c.1; SPBC11B10.02c.1:pep; SPBC11B10.02c.
DR   GeneID; 2539698; -.
DR   KEGG; spo:SPBC11B10.02c; -.
DR   PomBase; SPBC11B10.02c; his3.
DR   VEuPathDB; FungiDB:SPBC11B10.02c; -.
DR   eggNOG; KOG0633; Eukaryota.
DR   HOGENOM; CLU_017584_3_1_1; -.
DR   InParanoid; P36605; -.
DR   OMA; IWLNANE; -.
DR   PhylomeDB; P36605; -.
DR   UniPathway; UPA00031; UER00012.
DR   PRO; PR:P36605; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; TAS:PomBase.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IMP:PomBase.
DR   GO; GO:0010045; P:response to nickel cation; IMP:PomBase.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..384
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153508"
FT   MOD_RES         223
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   384 AA;  42734 MW;  83E02A8E46B5E122 CRC64;
     MFDLNTCLRK NILELQPYRC ARDDFSEGVL LDANECAYGS VISVDGVEFN RYPDPRQIEV
     KQRLCDLRNK ELSITKPLTP DNICMGVGSD EIIDSLIRIS CIPGKDKILM CPPSYGMYTV
     SAKINDVEVV KVLLEPDFNL NVDAICETLS KDSAIKVFFA CSPGNPTAKA LKLEDIKKIL
     EHPTWNGIVV VDEAYIDFSA PDMSALTLVN EYPNLAVCQT LSKSFGLAGI RIGFCLTSKP
     IATIMNSLKA PYNISEPTSR LALDALSPQS IDKMHTYRDA IIQQRVRLCK ELTTIKGMGK
     IIGGYDANFI LIQVLDRPEG GKPSNDAAKY LYLQMATMHK VVVRFRGTEP LCEGALRITV
     GTEEENTILL KTIKLVLQEY YTKK
 
 
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