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Database: UniProt
Entry: A0A0A2TIG0_9FIRM
LinkDB: A0A0A2TIG0_9FIRM
Original site: A0A0A2TIG0_9FIRM 
ID   A0A0A2TIG0_9FIRM        Unreviewed;       623 AA.
AC   A0A0A2TIG0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Polysaccharide biosynthesis protein {ECO:0000313|EMBL:KGP75414.1};
GN   ORFNames=JT05_10655 {ECO:0000313|EMBL:KGP75414.1};
OS   Desulfosporosinus sp. Tol-M.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1536651 {ECO:0000313|EMBL:KGP75414.1, ECO:0000313|Proteomes:UP000030439};
RN   [1] {ECO:0000313|EMBL:KGP75414.1, ECO:0000313|Proteomes:UP000030439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Abu Laban N., Tan B., Dao A., Foght J.;
RT   "Draft genome of Desulfosporosinus sp. Tol-M obtained by stable isotope
RT   probing of toluene- degrading methanogenic culture enriched from oil sands
RT   tailing of Alberta, Canada.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC       {ECO:0000256|ARBA:ARBA00007430}.
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:KGP75414.1}.
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DR   EMBL; JQID01000137; KGP75414.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2TIG0; -.
DR   STRING; 1536651.JT05_10655; -.
DR   Proteomes; UP000030439; 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   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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030439};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        41..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        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          290..573
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   623 AA;  68851 MW;  CFF37625B7777CBE CRC64;
     MLFRKRTWLL MLIDAMLINL AAFGSFYLRF VGDIKLEDYQ IYNHTAIAAT IIYIAVFYIF
     GLYNRLWQYA STGELLSIVY AVTVGTGGTA AAVYLYGVAT AAKLPFRIPN SASVLLWFSM
     VLLIGGSRFI WRILQDSRYD RHVPGSQKQV LIVGAGDAGV LAARELKNRN YRDGRPIGFI
     DDDRSKVKLK VLGIPVLGTR KDIVRAVKDH NVDEVIIAMP SASGESIREI VQICEKSGVD
     IKIMPGVYDI ISGDININPI RQVQVEDLLG RDPVSVDLEE VAGYVSGETV IITGAGGSIG
     SEICRQIARF NPGKLVLLGH GENSIFEIEQ ELRAEHPGID YITEILDIKD RQKVDLIFEK
     YKPGVVFHAA AHKHVPLMER NPEEALKNNV IGSQNLAEAA DKARVKTFVS ISTDKAVNPT
     SVMGASKRIV EMLIQSLDRH SQTRFVAVRF GNVLGSNGSV IPTFKRQIAK GGPVTVTHPD
     MVRYFMTIPE AAQLVIQAGA MAKGGEIFIL DMGKPVKIVD LAKDLIRLSG FEPDVDIKTQ
     FTGIRPGEKL FEELLTAEEG ITSTKHSRIF VAKPNGIDVK LLEELTHIIR ERGSYLTRNE
     VIELLQTVIP TFRKQAVKAV ANQ
//
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