ID A0A3S4SR27_9ACTO Unreviewed; 611 AA.
AC A0A3S4SR27;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=UDP-glucose 4-epimerase {ECO:0000313|EMBL:VEG75707.1};
DE EC=5.1.3.2 {ECO:0000313|EMBL:VEG75707.1};
GN Name=capD {ECO:0000313|EMBL:VEG75707.1};
GN ORFNames=NCTC11923_02382 {ECO:0000313|EMBL:VEG75707.1};
OS Actinomyces slackii.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=52774 {ECO:0000313|EMBL:VEG75707.1, ECO:0000313|Proteomes:UP000276899};
RN [1] {ECO:0000313|EMBL:VEG75707.1, ECO:0000313|Proteomes:UP000276899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11923 {ECO:0000313|EMBL:VEG75707.1,
RC ECO:0000313|Proteomes:UP000276899};
RG Pathogen Informatics;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC {ECO:0000256|ARBA:ARBA00007430}.
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DR EMBL; LR134363; VEG75707.1; -; Genomic_DNA.
DR RefSeq; WP_051281438.1; NZ_LR134363.1.
DR AlphaFoldDB; A0A3S4SR27; -.
DR STRING; 1278298.GCA_000428685_01372; -.
DR KEGG; asla:NCTC11923_02382; -.
DR Proteomes; UP000276899; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC.
DR CDD; cd05237; UDP_invert_4-6DH_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003869; Polysac_CapD-like.
DR PANTHER; PTHR43318:SF1; POLYSACCHARIDE BIOSYNTHESIS PROTEIN EPSC-RELATED; 1.
DR PANTHER; PTHR43318; UDP-N-ACETYLGLUCOSAMINE 4,6-DEHYDRATASE; 1.
DR Pfam; PF13727; CoA_binding_3; 1.
DR Pfam; PF02719; Polysacc_synt_2; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:VEG75707.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000276899};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 289..563
FT /note="Polysaccharide biosynthesis protein CapD-like"
FT /evidence="ECO:0000259|Pfam:PF02719"
FT REGION 588..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 66954 MW; 3ABF5AD3C6E46870 CRC64;
MRVSRRKAAA ALTADTLGWL VATLMVHALA DSGSLLALAG LGVFLLVAVS TNALLGTLVL
LTYRRRFRTS SFEEVSTLAA QYALSTLAGA LAVAAWAALT GGTVSILGLT LIPFLALAIG
LLLRFALRAQ RTYVKARAYQ RSAKDRDRVI ILGAGEVGNQ VVRLTKDDAA SPFLPVGLLD
DDETKKFLRL QGVPVMGTVD TVVECCQRED VRTVIIAIAD LPTDRLKQIT QDCAQAGIKT
MTIVPVREIA RKSLQFSDIK DIDLADVLGR REVNTDLSRI SEYITGRCVL VTGAGGSIGS
EIARQLHRLA PRELVLLDRD ESSLHSIQLG IYNKGLLDTR DMVLCDIRDK DALRKVFREH
RPDVVFHAAA LKHLPLLEQY PEEGWKTNVI GTKNVLELSR EFAVSTLVNV STDKAADPAS
VLGRTKHLAE QMTTSLALEH NLRFVSVRFG NVLGSRGSML WTFKHQIDAG GPVTVTDPDV
QRYFMTIPEA CELVLQAGAI GRPGDTMVLD MGDPVRIVDV ARRLIAQSGQ DITIEFTGLR
YGEKLSEDLI ASNEDDERPF HHLISHVQVE SVSPSSIEGL RTWTLDGYRP RAKDPERSSA
PMVTREKQAI R
//
