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Database: UniProt
Entry: B4WZ73_9GAMM
LinkDB: B4WZ73_9GAMM
Original site: B4WZ73_9GAMM 
ID   B4WZ73_9GAMM            Unreviewed;       639 AA.
AC   B4WZ73;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Polysaccharide biosynthesis protein {ECO:0000313|EMBL:EDX91207.1};
GN   ORFNames=ADG881_3309 {ECO:0000313|EMBL:EDX91207.1};
OS   Alcanivorax sp. DG881.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=236097 {ECO:0000313|EMBL:EDX91207.1, ECO:0000313|Proteomes:UP000003954};
RN   [1] {ECO:0000313|EMBL:EDX91207.1, ECO:0000313|Proteomes:UP000003954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG881 {ECO:0000313|EMBL:EDX91207.1,
RC   ECO:0000313|Proteomes:UP000003954};
RA   Bolch C., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) 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; DS989915; EDX91207.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4WZ73; -.
DR   STRING; 236097.ADG881_3309; -.
DR   eggNOG; COG1086; Bacteria.
DR   HOGENOM; CLU_013560_6_0_6; -.
DR   Proteomes; UP000003954; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   InterPro; IPR029063; SAM-dependent_MTases_sf.
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; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        102..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          277..570
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
FT   REGION          617..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   639 AA;  69129 MW;  7A0F72F3A91E7812 CRC64;
     MVSLSRTAKR LVMLSADALA APLLLWLAYG LRLNTATPEV ADLWLLVAAP LVLLPALYVL
     GFYRSIVRYL GAEVAWSILA GVTLSVVLLA AASYMASAST PRSVFIIFWA VLVLYLGGSR
     FMMRRFLYHV LGNRIDREAV AVFGAGGAGA QLVSGLLSTA ELHPLMIVDD AVGKQGTLLC
     GVPVVGRRAL EKAVERGAIR TVLLALPSES RATRMAVVRW LETLNVHVQT VPSFADIASG
     KARLEEIKEV AIEDLLGRDA VPPRADLLTR CISGKHVLVT GAGGSIGSEL CRQILKLSPS
     KLLLLDQSEF GLYAIEKELQ AFAGNRSKDI EIEAVLGSVV NRGLMERLCR EHRVDTVYHA
     AAYKHVPIVE ANPSAGVRNN ILGTLEAALG AEAAHVKHFI LVSTDKAVRP TNVMGATKRF
     AELVLQAIAA RGSETVFSMV RFGNVLGSSG SVVPLFRDQI QKGGPVTVTH PDVIRYFMTI
     PEASQLVIQA GAMAQGGEVF VLDMGEPVRI VDLARTMVHL MGMSVRDEKN PDGDIEIAFS
     GLRPGEKLYE ELLIGDCSTR TEHEMIMQAH EEKLEWDEIY FALEAFRKAL TRADQDALRA
     LLRSYVNGYE PGGLDIEAPQ SVPSREAPAL VAKTASAVE
//
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