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Database: UniProt
Entry: H2AU65_KAZAF
LinkDB: H2AU65_KAZAF
Original site: H2AU65_KAZAF 
ID   H2AU65_KAZAF            Unreviewed;       378 AA.
AC   H2AU65;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 47.
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   Name=KAFR0D02670 {ECO:0000313|EMBL:CCF57915.1};
GN   ORFNames=KAFR_0D02670 {ECO:0000313|EMBL:CCF57915.1};
OS   Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS   1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF57915.1, ECO:0000313|Proteomes:UP000005220};
RN   [1] {ECO:0000313|EMBL:CCF57915.1, ECO:0000313|Proteomes:UP000005220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC   NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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DR   EMBL; HE650824; CCF57915.1; -; Genomic_DNA.
DR   RefSeq; XP_003957050.1; XM_003957001.1.
DR   AlphaFoldDB; H2AU65; -.
DR   STRING; 1071382.H2AU65; -.
DR   GeneID; 13882577; -.
DR   KEGG; kaf:KAFR_0D02670; -.
DR   eggNOG; ENOG502QPT5; Eukaryota.
DR   HOGENOM; CLU_031468_10_2_1; -.
DR   InParanoid; H2AU65; -.
DR   OrthoDB; 1354873at2759; -.
DR   Proteomes; UP000005220; Chromosome 4.
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   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   Membrane {ECO:0000256|SAM:Phobius}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          10..172
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          217..360
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   378 AA;  42746 MW;  ED618208FAE698C0 CRC64;
     MTVNSRPVLH VLGMGSMGAL LAVNLLQTTR TEVIPLFRNT EKLSKFQNEG KSTISIRKVF
     LKEAPLVSAK LVRSYSPETF NDDHIENLVI TTKTYQTKEA IKPYLDFITP ETNIILIQNG
     LGVLEVLKDE VFVEQSKRPN LFQGVIGHGC YQDSAYIFNH AGNAGMKIAR LPWDDNMVQH
     ESVLKQDAVD NSLVKILMEK DFASIFNTTH MTYQEMLLGQ LQKFLVNSCI NPVTAILDCD
     NGEMVDYCKD IFTSIVEEEL NILGLAYRPL FEYEDHYKEQ TGYPNLDVKS TLNTESMVSN
     IINLGCVINA KNSSSMRQDT RYLRDSEIEY INGYIVKLAA KLNLNPNEAK TNRAICQLVN
     LRLGLNRTRA ATGDWPFK
//
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