UGA4E_THEGP
ID UGA4E_THEGP Reviewed; 323 AA.
AC F8C4X8;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=UDP-glucuronate 4-epimerase {ECO:0000303|Ref.2};
DE Short=UGA4E {ECO:0000303|Ref.2};
DE EC=5.1.3.6 {ECO:0000269|Ref.2};
DE AltName: Full=TgUGAE {ECO:0000303|Ref.2};
GN OrderedLocusNames=TOPB45_0660 {ECO:0000312|EMBL:AEH22762.1};
OS Thermodesulfobacterium geofontis (strain OPF15).
OC Bacteria; Thermodesulfobacteria; Thermodesulfobacteriales;
OC Thermodesulfobacteriaceae; Thermodesulfobacterium.
OX NCBI_TaxID=795359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF15;
RX PubMed=23580711; DOI=10.1128/genomea.00162-13;
RA Elkins J.G., Hamilton-Brehm S.D., Lucas S., Han J., Lapidus A., Cheng J.F.,
RA Goodwin L.A., Pitluck S., Peters L., Mikhailova N., Davenport K.W.,
RA Detter J.C., Han C.S., Tapia R., Land M.L., Hauser L., Kyrpides N.C.,
RA Ivanova N.N., Pagani I., Bruce D., Woyke T., Cottingham R.W.;
RT "Complete genome sequence of the hyperthermophilic sulfate-reducing
RT bacterium Thermodesulfobacterium geofontis OPF15T.";
RL Genome Announc. 1:E0016213-E0016213(2013).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX DOI=10.3390/catal10020222;
RA Gevaert O., Van Overtveldt S., Da Costa M., Beerens K., Desmet T.;
RT "Novel insights into the existence of the putative UDP-glucuronate 5-
RT epimerase specificity.";
RL Catalysts 10:222-222(2020).
CC -!- FUNCTION: Catalyzes the interconversion of UDP-D-glucuronic acid (UDP-
CC GlcA) and UDP-D-galacturonic acid (UDP-GalA). {ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucuronate = UDP-alpha-D-galacturonate;
CC Xref=Rhea:RHEA:11404, ChEBI:CHEBI:57635, ChEBI:CHEBI:58052;
CC EC=5.1.3.6; Evidence={ECO:0000269|Ref.2};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:Q14376};
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; CP002829; AEH22762.1; -; Genomic_DNA.
DR RefSeq; WP_013909462.1; NC_015682.1.
DR AlphaFoldDB; F8C4X8; -.
DR SMR; F8C4X8; -.
DR STRING; 795359.TOPB45_0660; -.
DR EnsemblBacteria; AEH22762; AEH22762; TOPB45_0660.
DR KEGG; top:TOPB45_0660; -.
DR PATRIC; fig|795359.3.peg.670; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_1_7_0; -.
DR OMA; EPIKVFN; -.
DR OrthoDB; 1180629at2; -.
DR Proteomes; UP000006583; Chromosome.
DR GO; GO:0050378; F:UDP-glucuronate 4-epimerase activity; IEA:UniProtKB-EC.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Isomerase; NAD; Reference proteome.
FT CHAIN 1..323
FT /note="UDP-glucuronate 4-epimerase"
FT /id="PRO_0000450328"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 11..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
FT BINDING 156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q14376"
SQ SEQUENCE 323 AA; 36622 MW; 5F839F094C417C9D CRC64;
MGYYLVTGVA GFIGWRVGEF LLKEGKAVLG VDNLNDAYDV TLKYWRLNEL KKSENFKFYQ
IDITNFQALK TIFETYSISA VIHLAARAGV RASLENPWVY VDSNITGTLN LLELMKDFGV
KKLVLASTSS IYAGQSPPFH EDLKVDTPLS PYAATKKGAE LLSYTYHHLY GLDISVVRYF
TVYGPAGRPD MSIFRFIKWI YEEKPIKIFG DGTQARDFTY IDDIARGTIA SLKPLGYEII
NLGGGKNPIS INQIIEILER LIGKKAKREY LNFHKADVKV TWADISKAKK LLNWEPEISI
EEGLKRTVNW SKENIELIKS IKV
