ID A0A142M5E6_AMIAI Unreviewed; 302 AA.
AC A0A142M5E6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=UDP-glucose 4-epimerase {ECO:0000313|EMBL:MBB3704085.1};
DE EC=5.1.3.2 {ECO:0000313|EMBL:MBB3704085.1};
GN ORFNames=FHS67_000379 {ECO:0000313|EMBL:MBB3704085.1};
OS Aminobacter aminovorans (Chelatobacter heintzii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Aminobacter.
OX NCBI_TaxID=83263 {ECO:0000313|EMBL:MBB3704085.1, ECO:0000313|Proteomes:UP000577697};
RN [1] {ECO:0000313|EMBL:MBB3704085.1, ECO:0000313|Proteomes:UP000577697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10368 {ECO:0000313|EMBL:MBB3704085.1,
RC ECO:0000313|Proteomes:UP000577697};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000256|ARBA:ARBA00007637}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MBB3704085.1}.
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DR EMBL; JACICB010000001; MBB3704085.1; -; Genomic_DNA.
DR RefSeq; WP_067959959.1; NZ_JACICB010000001.1.
DR AlphaFoldDB; A0A142M5E6; -.
DR STRING; 83263.AA2016_2641; -.
DR OrthoDB; 9801785at2; -.
DR Proteomes; UP000577697; Unassembled WGS sequence.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR PANTHER; PTHR43000:SF7; DTDP-D-GLUCOSE 4,6-DEHYDRATASE; 1.
DR PANTHER; PTHR43000; DTDP-D-GLUCOSE 4,6-DEHYDRATASE-RELATED; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:MBB3704085.1}.
FT DOMAIN 4..47
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 302 AA; 33733 MW; 1E518F81D5AA5F0D CRC64;
MTSILVTGGL GYTGRIIVRQ LAEQGFKVVN YNRDYSEWAT DLITPVQGEL YDIPRLVRTI
ERHEVDRVIH TAAMSHPDLS IELPVTTVVA NIDGTVNLME AMRLAGIRRL VNFSSETVYG
NHVEPIDERS ATVPTTPYGV TKVAVEHFSR IYNELYGLEA LCLRFSEVYG PGNRMPQILR
DIIKPVLRGQ AFRMENGADH LFHFIHAEDV GRAAILAAFA DKPDGSVFNV FGDRCWTLSE
AVGLIRKLLP QADIAIGPGY CHLDRQGPWD QSAARRALGY APGYTLEQGL AAYVEWLRSN
EY
//
