ID A0A0P1GW16_9RHOB Unreviewed; 693 AA.
AC A0A0P1GW16;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=UDP-N-acetyl-alpha-D-glucosamine C6 dehydratase {ECO:0000313|EMBL:CUH80781.1};
DE EC=4.2.1.135 {ECO:0000313|EMBL:CUH80781.1};
GN Name=pglF {ECO:0000313|EMBL:CUH80781.1};
GN ORFNames=TRM7557_03070 {ECO:0000313|EMBL:CUH80781.1};
OS Tritonibacter multivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=928856 {ECO:0000313|EMBL:CUH80781.1, ECO:0000313|Proteomes:UP000052022};
RN [1] {ECO:0000313|EMBL:CUH80781.1, ECO:0000313|Proteomes:UP000052022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7557 {ECO:0000313|EMBL:CUH80781.1,
RC ECO:0000313|Proteomes:UP000052022};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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; CYSD01000040; CUH80781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1GW16; -.
DR STRING; 928856.SAMN04488049_11619; -.
DR Proteomes; UP000052022; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; 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 Lyase {ECO:0000313|EMBL:CUH80781.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000052022};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 54..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 286..576
FT /note="Polysaccharide biosynthesis protein CapD-like"
FT /evidence="ECO:0000259|Pfam:PF02719"
FT REGION 653..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 73909 MW; 12BEAE95BC972CA0 CRC64;
MKLFLFLQRL TRGHKAGIVL SLDMVLLPLA LLFAFALQPQ PQSAFHLLGQ MLPTLPYVLG
SVAALSLWLG LPQIQLKAYE RHAVGQTVVV AASATAIEAT LCLIFGPDLA LGTHVVFGLC
YFLFMVAVRA VLYQVVLAIY RRVRPCRQVL IYGAGATGTQ LAQALKAHDQ ITPVAFIDDN
VSLQGVTLVG LPVLAPGEIA ALARDRDISR VLLAMPSQSQ PKQVQIIQRL QKLGLEVQAL
PSFAQLIGEE ALVDKLKPVA PQNFLGRDTR SLSLNEASSS YTGRVVLVSG AGGSIGSELC
RQVLACRPAK LVLYELSELA LYTIHQELSQ VVDGTLIELV PVLGSVTDPR QVRRVLADHE
VQVVLHAAAY KHVPLVEANP LPGLANNVFG TRTLARAAAD QGVERFILIS SDKAVRPTNV
MGASKRLAEL VVQDQAARGS DTVFTMVRFG NVLGSSGSVI PLFQEQIARG GPVTVTDPRV
KRYFMTISEA VQLVLQAGAK ARGGEVFVLD MGEPISILQL ARQVIEAAGY AVRDEKRPDG
DIEINIIGLR PGEKLEEELT ICEELITTGH PKIFCAREAV LSEIEVAGFL RNLRQVVAAG
DELAAKTLIA RWVEGYGAAL ADQQLSRGDA LAGVPARAGY AVGTDREAAL EAGLDPAGAD
FADPGADPAA DQGVDRGKRA PKTTPQSAGG LGV
//
