ID A0A163BSC6_DIDRA Unreviewed; 869 AA.
AC A0A163BSC6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE SubName: Full=2-dehydropantoate 2-reductase {ECO:0000313|EMBL:KZM21949.1};
GN ORFNames=ST47_g6929 {ECO:0000313|EMBL:KZM21949.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM21949.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM21949.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM21949.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
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:KZM21949.1}.
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DR EMBL; JYNV01000231; KZM21949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163BSC6; -.
DR STRING; 5454.A0A163BSC6; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 NCBIfam; TIGR00745; apbA_panE; 1.
DR PANTHER; PTHR21708:SF30; 2-REDUCTASE FAMILY PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G00740)-RELATED; 1.
DR PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 440..458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..161
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 188..311
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 762..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 95137 MW; DC10BDE64E419847 CRC64;
MTGNTQPNVL LFGAGGVGTV YLWLLSKSST TTAVCRSNYD VAKEDGFIIN SSIFGQGIHF
RPNVVRSCEE AASANETPYD YIVVCSKAIP DTVPKWIAPV VTPGHTTIVL LQNGVGIEEE
YRVAFPSNPI VSTVLYFPAT QRPAGVIKHG EVERLEIGAY PSSASAEHAK AFAQLVQSAG
ATAILHEDIQ LIRWTKLLIN ASWNPICALS FSKDTDVLES YDGAPDIIEA VMLEIRDIAV
AYGYNITEEK VKFELNRAKA RIPIHAGIEP SMLQDVQTGR RIEVEAIVGN PVRMGRAKGV
KCDRLELLIQ AALVFDIGPF PALLSWLNYT FLIALLLTTT PKLPNGPPIT ATSSKQLRFP
AKMTTDSSLS LLFSIVAFLF ECVVLLCMSP LIGSGPLQAV MKTAVRTLLG SPGKFEYLLE
LEYDDHIGDS PSNTWEACQY LCIIAIMSLP AAATYFIFST CMFQWKLHST RTDGPKSSEG
SVNTLPTSQS PTILRSCCRT LRTMRRVAAE TCLAIAHLVY MARAFHLSLN LRFKHLQSSW
PNLSHTRTSN PSAAANVLPD NWGLFSLYQP PIEGRSLKKT YNKKAATIDA VASDAMQLVS
QTEKDISMAD LSSISTPESS ELFQSLLTAV SERANIVEAS KQHRSIFLRM VEEKLTAITP
LSVHAQDLHQ CIWIQMLSSF YTELQPHCYL FQEHGDDVLM SLLRNICHFG NHLGLQFQPP
NFTRPGTPPA ATHQQPKGFV STTGGQQAAI SAVTFPPVQT QRLPAMSQQS PSGPRSGTGR
LQAGTSVAVK PMDLGFAAST LNFGITEEEF TPARRKQTTA KQHRALRPTA TRTSPKGAVS
RSCPNQSSSH EPTFEEILED QMIAEFSAQ
//