ID B6QH48_TALMQ Unreviewed; 764 AA.
AC B6QH48;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=2-dehydropantoate 2-reductase, putative {ECO:0000313|EMBL:EEA22693.1};
GN ORFNames=PMAA_093120 {ECO:0000313|EMBL:EEA22693.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA22693.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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DR EMBL; DS995902; EEA22693.1; -; Genomic_DNA.
DR RefSeq; XP_002148860.1; XM_002148824.1.
DR AlphaFoldDB; B6QH48; -.
DR VEuPathDB; FungiDB:PMAA_093120; -.
DR HOGENOM; CLU_021479_0_0_1; -.
DR OrthoDB; 2727909at2759; -.
DR PhylomeDB; B6QH48; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
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 PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR21708:SF25; PROTEIN PAM1-RELATED; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001294}.
FT DOMAIN 10..166
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 199..322
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 333..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..349
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 82890 MW; 99E8E43D036D7AA2 CRC64;
MAPSPPRLRI LSVGSNAVSA FLSWRLQTTN SCDVTLAWKS GFESVAQYGV SFRSKTYGNE
RFKPRHVVRT PEEAASREVA YDYVVLCVKA LPDIYDLGSI IESVVTPQHT CILVNTTNTL
GVESHLEQRF PTNVVLSLVS HMTINQTGLS DFEHEGSTEM WVGPANKNPA IPVSIQNDMA
SALAMTLSSG NVDCKVSSNI RQEQFDRMIG PIAFHPASVL FNTPNHSQLL EKVGVRQLVN
DVIDELLKLA STQGCSFDSG YREKVIAKMT APTEAQTTMY QDFLAHRPME IETYLASPIR
LAMESNVSLP RIETIYAMLH HLNIVNQTKP EILPPGISTQ PPPRTASVPP GQKPMVNGMR
ASRTSSNMGM PMPPPQQRRG PPPGGPMLRP PSAQAGPSRM PRDASFEDNG LEEFSHLVVY
DDIPSDGLTN GNMDMANGGA SSSLALRERE LALRQRELQL REREMNLRRG PGPRGGPRAP
PPPRSVFDEE DEEDYFDPQD FRPPPGIDID NIDMMSVTSR RTRKAPTSAG QLRRNPEMNG
PPSSRPSSSF RFFNGSGGRK SASSHLINDI PMTHSSLMDD PLMAYSSNRY GAVDRKELHV
DSRANSLSNA SRMGDFGPGG APGSYPPGRR TSGSPAVFPN GRGMPMPRPG PGEHQHSWGP
PPNGMMPPHG RPSPPNVSPG MPPNMRAPVP RYPPGHGNNM GANQVEQHLG VSNPPKYNSP
NARSLTGSAS ASAESGDSGA SANIDSENSA HSSQISLGHA MPVR
//
