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
//