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PANB_EMENI
ID   PANB_EMENI              Reviewed;         349 AA.
AC   Q9Y7B6; C8VPD6; Q5BCF2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=3-methyl-2-oxobutanoate hydroxymethyltransferase;
DE            EC=2.1.2.11 {ECO:0000269|PubMed:10503542};
DE   AltName: Full=Ketopantoate hydroxymethyltransferase;
GN   Name=panB; ORFNames=AN1778;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RX   PubMed=10503542; DOI=10.1007/s004380051065;
RA   Kurtov D., Kinghorn J.R., Unkles S.E.;
RT   "The Aspergillus nidulans panB gene encodes ketopantoate
RT   hydroxymethyltransferase, required for biosynthesis of pantothenate and
RT   Coenzyme A.";
RL   Mol. Gen. Genet. 262:115-120(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-
CC         oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-
CC         dehydropantoate; Xref=Rhea:RHEA:11824, ChEBI:CHEBI:11561,
CC         ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:57453; EC=2.1.2.11;
CC         Evidence={ECO:0000269|PubMed:10503542};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 1/2.
CC   -!- SIMILARITY: Belongs to the PanB family. {ECO:0000305}.
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DR   EMBL; AF134703; AAD37248.1; -; Genomic_DNA.
DR   EMBL; AACD01000028; EAA63954.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF85545.1; -; Genomic_DNA.
DR   PIR; T50553; T50553.
DR   RefSeq; XP_659382.1; XM_654290.1.
DR   AlphaFoldDB; Q9Y7B6; -.
DR   SMR; Q9Y7B6; -.
DR   STRING; 162425.CADANIAP00008425; -.
DR   EnsemblFungi; CBF85545; CBF85545; ANIA_01778.
DR   EnsemblFungi; EAA63954; EAA63954; AN1778.2.
DR   GeneID; 2874758; -.
DR   KEGG; ani:AN1778.2; -.
DR   VEuPathDB; FungiDB:AN1778; -.
DR   eggNOG; KOG2949; Eukaryota.
DR   HOGENOM; CLU_036645_0_1_1; -.
DR   InParanoid; Q9Y7B6; -.
DR   OMA; VLVWTDM; -.
DR   OrthoDB; 1439584at2759; -.
DR   BRENDA; 2.1.2.11; 517.
DR   UniPathway; UPA00028; UER00003.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003864; F:3-methyl-2-oxobutanoate hydroxymethyltransferase activity; IDA:AspGD.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IDA:AspGD.
DR   CDD; cd06557; KPHMT-like; 1.
DR   Gene3D; 3.20.20.60; -; 1.
DR   HAMAP; MF_00156; PanB; 1.
DR   InterPro; IPR003700; Pantoate_hydroxy_MeTrfase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR20881; PTHR20881; 1.
DR   Pfam; PF02548; Pantoate_transf; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   TIGRFAMs; TIGR00222; panB; 1.
PE   1: Evidence at protein level;
KW   Pantothenate biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..349
FT                   /note="3-methyl-2-oxobutanoate hydroxymethyltransferase"
FT                   /id="PRO_0000184925"
SQ   SEQUENCE   349 AA;  37643 MW;  211C4A15309BA25A CRC64;
     MTFLRIATKR AIYLHRPANP ALPTSSILPV LHSTNVATRV PSPCAIRHSS HSPLGAAQAN
     PRKKVTMQTL RNLYKKGEPI TMLTAHDFPS AHVADAAGMD MILVGDSLAM VALGMQDTSE
     VTLDDMLVHC RSVARAAQSA FTVSDLPMGS YEVSPEQALQ SAIRIVKEGR VQGVKLEGGE
     EMAPAIKRIT TAGIPVVGHI GLTPQRQNAL GGFRVQGKST TDALKLLKDA LAVQEAGAFM
     IVIEAVPPEI ASIVTQKLSV PTIGIGAGNG CSGQVLVQID MTGNFPPGRF LPKFVKQYAN
     VWNEALQGIQ QYREEVKSRA YPAEQHTYPI PKEELVEFQK AVDELPEEK
 
 
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