ID A0A177CTK3_9PLEO Unreviewed; 530 AA.
AC A0A177CTK3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00013014};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN ORFNames=CC84DRAFT_1112909 {ECO:0000313|EMBL:OAG10521.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG10521.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG10521.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG10521.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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DR EMBL; KV441549; OAG10521.1; -; Genomic_DNA.
DR RefSeq; XP_018040886.1; XM_018175335.1.
DR AlphaFoldDB; A0A177CTK3; -.
DR STRING; 1460663.A0A177CTK3; -.
DR GeneID; 28758821; -.
DR InParanoid; A0A177CTK3; -.
DR OrthoDB; 1354873at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR GO; GO:0015940; P:pantothenate biosynthetic process; 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; IPR003710; ApbA.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00745; apbA_panE; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT DOMAIN 52..247
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 320..452
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..289
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 58250 MW; 5062B2CE0201A0D1 CRC64;
MRSWLGPEST EPQAKQGINA EKDAVSLPDD TPTMPRNPAE FYRAQPVRDR RIHIMGLGNV
GYFVAHSLKG IPNAPPIALV FHSREKLKAW EESSKRLQCI TDGDTERREG YDAELALPRP
RSHGKLVGSN TGDPFPDASD ANERISEGSI MFGESTEPIS SLILCMKATQ VLSALSSVKH
RLHRDSVICF LQNGMGTVEE VNKEIFPDIA TRPHYMVGIN SHGMKKTDDP FTVVHAGFGT
ISLGILPNER DRAPAPYAPI SKFTPHSSPQ PIEPVHPANP DPSAPPATDP SATFTPNSRY
LLRTLLRTPV LCAAGFSPPD LLQLQLEKLA VNCIVNPLTV MLDARNGSIL YNYSLTRVMR
LLLSEISLVI RSLPELQYIP NVQQRFDPGR LETVVVGVAN RTSDNISSML ADVRAGRQTE
MDYINGWIVN KGEEMGIKCF MNFMLMHMVK GKSGMIQAEL GEGIPFVEPR PGEEAVMTRD
AFGDIPFADV ISRDMSTSEE AKTKNASGDI PPADSVAGKT SNPEWTEKSR
//
