ID A0A132C3F5_9RHOB Unreviewed; 634 AA.
AC A0A132C3F5;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=UDP-N-acetyl-alpha-D-glucosamine C6 dehydratase {ECO:0000313|EMBL:KUP95056.1};
DE EC=4.2.1.135 {ECO:0000313|EMBL:KUP95056.1};
GN Name=pglF {ECO:0000313|EMBL:KUP95056.1};
GN ORFNames=TRIHO_00560 {ECO:0000313|EMBL:KUP95056.1};
OS Tritonibacter horizontis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=1768241 {ECO:0000313|EMBL:KUP95056.1, ECO:0000313|Proteomes:UP000068382};
RN [1] {ECO:0000313|EMBL:KUP95056.1, ECO:0000313|Proteomes:UP000068382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O3.65 {ECO:0000313|EMBL:KUP95056.1,
RC ECO:0000313|Proteomes:UP000068382};
RA Poehlein A., Giebel H.A., Voget S., Brinkhoff T.;
RT "Genome sequence of the marine Rhodobacteraceae strain O3.65, Candidatus
RT Tritonibacter horizontis.";
RL Submitted (DEC-2015) 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:KUP95056.1}.
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DR EMBL; LPUY01000007; KUP95056.1; -; Genomic_DNA.
DR RefSeq; WP_068239103.1; NZ_LPUY01000007.1.
DR AlphaFoldDB; A0A132C3F5; -.
DR PATRIC; fig|1768241.3.peg.55; -.
DR OrthoDB; 9803111at2; -.
DR Proteomes; UP000068382; 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:KUP95056.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000068382};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..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 118..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 286..584
FT /note="Polysaccharide biosynthesis protein CapD-like"
FT /evidence="ECO:0000259|Pfam:PF02719"
SQ SEQUENCE 634 AA; 68550 MW; DF9864A93CA8F941 CRC64;
MSTFNLISGL SRSKKSGVFL GIDLLLLPLA LLFTYTVQDQ PVAPLTLLGQ MFPILPYILI
ATGGLSYWLG LPQVQLIAYE RHAMGQTAVV AVSAAAMEAV LCRIFGPQVP PGVHVVFAIS
YLIMMVAVRG VLYQIVLAVY RRARPRARVV IYGAGNTGTQ LAQALKAHDG IDPVAFVDDN
KSLQGLTLVG LPVCAPARIA ELVKTRDVKR VLLAMPSQNQ PKQAQIIQRL QKLGLEVQAL
PSFAQLIGEE ALVDKLTPVP PQNFLRRASR DVPMKEAAVS YADRVVLVSG AGGSIGSELC
RQVLACRPAK LVLYELSELA LYTIHQELCQ QLEGTGIELV PVLGSVTDPR QVRRVLVNHQ
VQVVLHAAAY KHVPLVEANP LAGLANNVFG TQTLARAAAE FGVERFILIS SDKAVRPTNV
MGASKRMAEL VVQDLASRSA PYGDGSAGHT VFTMVRFGNV LGSSGSVIPL FQEQISRGGP
VTVTDPRVKR YFMTIREAVQ LVLQAGAEAK GGEVFVLDMG EPVSILQLAR QVIESAGYSV
RDDDHPEGDI AIDIIGLRPG EKLEEELTLS TELITTRHPK IFCAREAVLS EIEVAALLRA
LRQVVASGDS EGARRVIMRW VEGYVQPLAD RKSS
//
