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
//