ID A0A177D219_ALTAL Unreviewed; 490 AA.
AC A0A177D219;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=CC77DRAFT_1026560 {ECO:0000313|EMBL:OAG13546.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG13546.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG13546.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG13546.1,
RC ECO:0000313|Proteomes:UP000077248};
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; KV441509; OAG13546.1; -; Genomic_DNA.
DR RefSeq; XP_018378967.1; XM_018526285.1.
DR AlphaFoldDB; A0A177D219; -.
DR STRING; 5599.A0A177D219; -.
DR GeneID; 29111879; -.
DR KEGG; aalt:CC77DRAFT_1026560; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1026560; -.
DR OMA; RKEPFQV; -.
DR OrthoDB; 1354873at2759; -.
DR Proteomes; UP000077248; 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:UP000077248}.
FT DOMAIN 49..236
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 311..443
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 54599 MW; 046DE2D3183FDF1F CRC64;
MTSRKKSESV GAQNELADGK DRPDQSVPSP ASHNTADFYR RQSVLDRRVH IMGIGNVGKF
IAHALRGIPN APPVTLIFGG WEKYNEWNNS QQRLTLVTEG DAEIRDGYDA ELAIPRVRYH
GQEVGLNASS VDAPGGPRIL PGESTEPISS LIICLKAPFV LQAISSVKHR LHKDSVVCFL
QNGMGVIEEV NREIFPDPET RPHYILGINS HGMHTSRDGR FTTVHAGFGT ISLGILPHER
DRNPNEPYVP ELRFTAPKDS KPFYPDEPDK LNPEYPPPSS GKFPFTPNQR YLLRTLLRTP
VLSAASFSPP DLLQMQLDKL AVNCIINPLT ALLDARNGAV LNNYALTRTM RLLLSEISLV
IRSLPELQYI PNVSQRFDPG RLETVVVAVA HRTRDNVSSM LADTRQGAQT EIDYINGWVV
KRGEELGIRC AMNYMIMQLV KGKRMVVQHE MEEGVPLVEE KKGGRAEADL VVKRGQAEAS
KEDAREKEKL
//
