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Database: UniProt
Entry: A0A139ICF1_9PEZI
LinkDB: A0A139ICF1_9PEZI
Original site: A0A139ICF1_9PEZI 
ID   A0A139ICF1_9PEZI        Unreviewed;      1479 AA.
AC   A0A139ICF1;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AC579_5661 {ECO:0000313|EMBL:KXT12275.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT12275.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT12275.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT12275.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXT12275.1}.
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DR   EMBL; LFZO01000157; KXT12275.1; -; Genomic_DNA.
DR   STRING; 113226.A0A139ICF1; -.
DR   Proteomes; UP000073492; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        860..884
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1156..1267
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          1327..1458
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          498..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          811..853
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1134..1165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        521..611
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1139..1155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1479 AA;  157417 MW;  8D224409AAB08FB6 CRC64;
     MKALTGALID AAAAVEVFAG GDGGGNGDGI YSTWVESSAQ YEYSTKVWQK PCTTTAIWSH
     AAETSVYTTT SISIVDNTQS ITVSVPCTTT LPAVVSTSTS VYTSPTTEVI TSTSYIYSTY
     TSLVTVTEVT TQNTTIVSAT TETKLSSITL SASVLTLPGT TKTLPPSLVP TTVVDTSVQS
     ITVDNTILRY TTIVDQETIV NTITLSASVL TLPGTTETLP PSLVPTTVVD TSVQSITVDN
     TILRYTTIVD QETIVNTITI PAPPPVTVTV PTTVPTTITA TPSSALCPLG GPSSANSLGC
     GGRGCTVEFQ QEALVHWSEY PDSPPLVTVL SFVDESASAT CITTKCNTEV FNQYYRQTAT
     NCAYPPCPTN TIDCNCNIVV GPIGLPGGST TSVTQIGPSG WNLILGAVPT GRNIGLCLPD
     GGSCVTATST TLSTQLVYTG EVSSTVYNNA SAPQSTAWYL PELGEYFPLD SPFGACTTAL
     LRDTDVVAKH RKRQIAASNI SPWSGAPKNT RTLRPRVASE AVTEGSSQQT TPASTSVTTT
     PPSQPSNPTT TPVSSTSPTT EPTEPTVVET SPTSTPPSSE PTSTESGATS GETSSSIPIG
     TSTESPSSYS THSGTVYITE TVYYSMILSP GSAEATRSRG PSRSHSLPCA MRNHQHPGLS
     FILLLLSLLV NNVWATGVTI TSPAGGGTWP AGPITVKWED GGGMPDMAQL TTFVLELLVG
     GNLPSNSKVI ATLGGGHGKI QDGSVEDNIA ADVAQSIENG FYFRMTSNTS SGDQVINYSN
     RFTLIKLNGT TDSPYLDGAN AVAGMDDVPS SQYNQIARPS TTSGSPTSSA SATGTATTTT
     TATATSQPAS DDGLTTGVKV GIGVGACLAV IGVISLFGWA YVFWRHKKRK QRQQTQHPLN
     SARVSKYGAG VFLGNKVELP TDHAESSRSR LELSPTDERY EIHGSGKAVE AARASIYELE
     GDWSGWEAGN GRKSKAYDPT AIRAYRLGQN RTYAQSTEAE EKHRQKQESH IRKAMSAADI
     QYAPQTGVPS KRIHILGTGS IGKLVAHALR GIHDPPPVTL LLHRAQLLSA WISSKKVITV
     QDGDDVIARG GFDVEFSPPF RRQHGVVVED GRPEVWDTAD QTGMKPHEVA KMIQRQRREA
     GDGSSSASGS RSVDTNDPTY RKRSGYDAIS NEPIYNLIVT TKTPRTIAAL LSVKHRITKE
     TTICFLQNGM GIVEEANKEV FPDESTRPSY IQGIISHGAN IPLSKAEEDP FFVVHAGHGT
     VQLGAIPRRT TGWREAATPS GLGTENAGKL SETQLDNDEV SPTGRYIIRT LTRTPILAAV
     AFTPIELLQL QLEKLAINSV LNPMTALLDN RNGAILYNFA LSRVMRLLLA ETSLVIRSLP
     ELRGLPNVPH RFASDRLEGL VVAVANKTRD NISSMLADVR RGAPTEVEYI NGYIVKRGEE
     LGIKPVVNYS FMQMVIGKQF MVKREMDEEI PQATDHNRE
//
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