ID I2H8Y0_TETBL Unreviewed; 701 AA.
AC I2H8Y0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=NAD-dependent epimerase/dehydratase domain-containing protein {ECO:0000259|Pfam:PF01370};
GN Name=TBLA0I01740 {ECO:0000313|EMBL:CCH62832.1};
GN ORFNames=TBLA_0I01740 {ECO:0000313|EMBL:CCH62832.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH62832.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH62832.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
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 -!- FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is
CC active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and
CC lactose. {ECO:0000256|ARBA:ARBA00037676}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose;
CC Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914;
CC EC=5.1.3.2; Evidence={ECO:0000256|ARBA:ARBA00000083};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000256|ARBA:ARBA00004947}.
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000256|ARBA:ARBA00005028}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the aldose epimerase
CC family. {ECO:0000256|ARBA:ARBA00038238}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NAD(P)-dependent
CC epimerase/dehydratase family. {ECO:0000256|ARBA:ARBA00037955}.
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DR EMBL; HE806324; CCH62832.1; -; Genomic_DNA.
DR RefSeq; XP_004182351.1; XM_004182303.1.
DR AlphaFoldDB; I2H8Y0; -.
DR STRING; 1071380.I2H8Y0; -.
DR GeneID; 14498009; -.
DR KEGG; tbl:TBLA_0I01740; -.
DR eggNOG; KOG1371; Eukaryota.
DR HOGENOM; CLU_007383_22_0_1; -.
DR InParanoid; I2H8Y0; -.
DR OMA; KGLYREW; -.
DR OrthoDB; 5489993at2759; -.
DR Proteomes; UP000002866; Chromosome 9.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:InterPro.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-KW.
DR CDD; cd09019; galactose_mutarotase_like; 1.
DR CDD; cd05247; UDP_G4E_1_SDR_e; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR InterPro; IPR018052; Ald1_epimerase_CS.
DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR047215; Galactose_mutarotase-like.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005886; UDP_G4E.
DR NCBIfam; TIGR01179; galE; 1.
DR PANTHER; PTHR43725; UDP-GLUCOSE 4-EPIMERASE; 1.
DR PANTHER; PTHR43725:SF51; UDP-GLUCOSE 4-EPIMERASE; 1.
DR Pfam; PF01263; Aldose_epim; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023144};
KW Galactose metabolism {ECO:0000256|ARBA:ARBA00023144};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Reference proteome {ECO:0000313|Proteomes:UP000002866}.
FT DOMAIN 14..270
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
SQ SEQUENCE 701 AA; 78776 MW; 3CD0FD9ED7348DA5 CRC64;
MTQHTPTQPQ KKYVLVTGGA GYIGSHTVAE LIENGYECIV VDNLDNSSYE SVSRLQILTK
HKITFYHTDL CDKEELRKIF VNHNIDSVIH FAGLKAVGES TQIPLKYYRN NILGTLALLE
LMQEYHVEKL VFSSSATVYG DATRFPDMIP IPEECPLGPT NPYGNTKYTI EKILNDLYES
EKKNWKFAIL RYFNPIGAHP SGLIGEDPLG IPNNLLPYMA QVAVGRREKL NVFGNDYDSR
DGTPIRDYIH VVDLAKGHIA ALKYLDNTKS EGLCREWNLG SGTGSTVLEV YRAFCDACGD
DIPYEITGRR AGDVLNLTAK PDRATNELHW KTELNVADAC KDLWKWTTEN PFGYQLKGVV
DKFAAQKDDF ESRFITLGEG TKFEVTFANL GATIVDIKVD GQSVVLGYKD EAGYLQEDTA
YIGATIGRYA NRIAKGKYTL NGKEYQLTIN NGENCNHGGP STFHTKKFMG PLVQNPKKDI
FTAEFLLLDF GKELNEFPGD LIIHVKYIVN VAEKTLDIEY QAELVNGEAT PINMTNHTYF
NLNKVNKETF AGTELRVASA RSLDMDMKRV VPTGKIITRE IATFDSSKPT VLGEKTPDYD
YAFVIDENEK ITDVNTAKRR KLTTVAKAYH PESKIGLEIL TTEPTFQIYT GDWLSAGYTP
RQGFAVEPGR YVDAINHEQW RESVILKRGD VYGSKIVYRF T
//
