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
//