ID A0A162I0A7_9EURO Unreviewed; 482 AA.
AC A0A162I0A7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 05-FEB-2025, entry version 32.
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=AAP_06063 {ECO:0000313|EMBL:KZZ86943.1};
OS Ascosphaera apis ARSEF 7405.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ascosphaeraceae; Ascosphaera.
OX NCBI_TaxID=392613 {ECO:0000313|EMBL:KZZ86943.1, ECO:0000313|Proteomes:UP000242877};
RN [1] {ECO:0000313|EMBL:KZZ86943.1, ECO:0000313|Proteomes:UP000242877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 7405 {ECO:0000313|EMBL:KZZ86943.1,
RC ECO:0000313|Proteomes:UP000242877};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(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:KZZ86943.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZGZ01000042; KZZ86943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162I0A7; -.
DR VEuPathDB; FungiDB:AAP_06063; -.
DR OrthoDB; 73846at2759; -.
DR Proteomes; UP000242877; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR050838; Ketopantoate_reductase.
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:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR43765; 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000242877}.
FT DOMAIN 169..263
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 330..461
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 148..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 482 AA; 53680 MW; D0D357B6029DFEBB CRC64;
MQVPLLLSTS AKRCVPFARI PYQSQLWTFT STRRFSRHPL AMKQQQTGSA ADFFTSDAET
LLPPSQRVHI LGMGNIGCFI AHSLRGILNP PQVTLLLHNE NLYDQWWKQK RRVTLVKHGL
IEHAKGFDVS VARQGRWYTP SQPAIASRTS ADIANSSDEE LDTSTERSNP KTWALDEEPI
DNVILTCKAT QVEKALKSIA HRLLPTSTIV FLQNGMGIID EVNEKIFSDP SMRPNYISGI
TTHGFYRVEP FKAVHTGMGV TALAVTHTNS YIAGVEEVRH TQDETDPSIP TAKKTGDNNY
ELHSHTSRYL LSLLCRTPAL TATALDKTAI ITSQLEKLAM NCVINPLTVL FNCKNGDLLQ
SFNVARMQRL ILIEFAAVVR AMPELQGLPG LSVRFSPERL RKLAVGLERT TAENTSSMLQ
DVLGGRETEI DYINGYIVKK GDELGIRCVA NYMVMQAVLA KSRLGSKAAQ EVIPFENLEE
FL
//
