位置:首页 > 蛋白库 > PANC_ORYSJ
PANC_ORYSJ
ID   PANC_ORYSJ              Reviewed;         313 AA.
AC   O24210; A0A0P0W5L1; Q10AH8; Q851Y0;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Pantoate--beta-alanine ligase;
DE            EC=6.3.2.1;
DE   AltName: Full=Pantoate-activating enzyme;
DE   AltName: Full=Pantothenate synthetase;
GN   Name=PANC; OrderedLocusNames=Os03g0851800, LOC_Os03g63490;
GN   ORFNames=OSJNBa0015N08.21;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. Nipponbare; TISSUE=Seedling root;
RX   PubMed=10417331; DOI=10.1042/bj3410669;
RA   Genschel U., Powell C.A., Abell C., Smith A.G.;
RT   "The final step of pantothenate biosynthesis in higher plants: cloning and
RT   characterization of pantothenate synthetase from Lotus japonicus and Oryza
RT   sativum (rice).";
RL   Biochem. J. 341:669-678(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine to
CC       form pantothenate. Essential for panthotenate biosynthesis (Probable).
CC       {ECO:0000305|PubMed:10417331}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP +
CC         diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1;
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA71303.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA71303.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y10253; CAA71303.1; ALT_SEQ; mRNA.
DR   EMBL; AC096688; AAO20059.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF99935.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF13832.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS87394.1; -; Genomic_DNA.
DR   EMBL; AK066656; BAG90070.1; -; mRNA.
DR   PIR; T03924; T03924.
DR   AlphaFoldDB; O24210; -.
DR   SMR; O24210; -.
DR   STRING; 4530.OS03T0851800-01; -.
DR   PaxDb; O24210; -.
DR   PRIDE; O24210; -.
DR   EnsemblPlants; Os03t0851800-01; Os03t0851800-01; Os03g0851800.
DR   Gramene; Os03t0851800-01; Os03t0851800-01; Os03g0851800.
DR   eggNOG; KOG3042; Eukaryota.
DR   InParanoid; O24210; -.
DR   OMA; CNHKLEP; -.
DR   BRENDA; 6.3.2.1; 4460.
DR   PlantReactome; R-OSA-1119394; Pantothenate and coenzyme A biosynthesis III.
DR   PlantReactome; R-OSA-1119496; Pantothenate biosynthesis I.
DR   PlantReactome; R-OSA-1119544; Pantothenate biosynthesis II.
DR   PlantReactome; R-OSA-1119568; Pantothenate biosynthesis III.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   ExpressionAtlas; O24210; baseline and differential.
DR   Genevisible; O24210; OS.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblPlants.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IEA:EnsemblPlants.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IBA:GO_Central.
DR   CDD; cd00560; PanC; 1.
DR   Gene3D; 3.30.1300.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00158; PanC; 1.
DR   InterPro; IPR003721; Pantoate_ligase.
DR   InterPro; IPR042176; Pantoate_ligase_C.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR21299:SF1; PTHR21299:SF1; 1.
DR   Pfam; PF02569; Pantoate_ligase; 1.
DR   TIGRFAMs; TIGR00018; panC; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW   Pantothenate biosynthesis; Reference proteome.
FT   CHAIN           1..313
FT                   /note="Pantoate--beta-alanine ligase"
FT                   /id="PRO_0000128300"
FT   ACT_SITE        43
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         36..43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="beta-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57966"
FT                   /evidence="ECO:0000250"
FT   BINDING         178..181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000250"
FT   BINDING         215..218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   313 AA;  34039 MW;  8079519175263FDF CRC64;
     MAAPREPEVI RDKAAMRAWS RRRRAEGKTV AVVPTMGYLH QGHLSLISAA AAAASADPVA
     IVVTIYVNPS QFAPSEDLAT YPSDFAGDLR KLASTGVVDA VFNPPDLYVR GAGRRGAASG
     GAISCLEEAA GDGHETWVRV ERLEKGMCGA SRPVFFRGVA TIVSKLFNII EPDVAVFGKK
     DYQQWRVICR MVRDLDFAIE IIGSEIVREA DGLAMSSRNV HLSREEREKA LSISRSLVDA
     RTGALKGNTD CKQIKNKIVQ TLTETGGQVD YVEIVEQESL VPVEQIDGPV VICVAAWFGK
     VRLIDNIEID TRS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024