ID   A0A2R8AEI8_9RHOB        Unreviewed;       637 AA.
AC   A0A2R8AEI8;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=UDP-N-acetyl-alpha-D-glucosamine C6 dehydratase {ECO:0000313|EMBL:SPF30654.1};
DE            EC=4.2.1.135 {ECO:0000313|EMBL:SPF30654.1};
GN   Name=pglF {ECO:0000313|EMBL:SPF30654.1};
GN   ORFNames=POI8812_02996 {ECO:0000313|EMBL:SPF30654.1};
OS   Pontivivens insulae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pontivivens.
OX   NCBI_TaxID=1639689 {ECO:0000313|EMBL:SPF30654.1, ECO:0000313|Proteomes:UP000244932};
RN   [1] {ECO:0000313|EMBL:SPF30654.1, ECO:0000313|Proteomes:UP000244932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CeCT 8812 {ECO:0000313|EMBL:SPF30654.1,
RC   ECO:0000313|Proteomes:UP000244932};
RA   Keele B.F.;
RL   Submitted (MAR-2018) 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; OMKW01000004; SPF30654.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R8AEI8; -.
DR   OrthoDB; 9803111at2; -.
DR   Proteomes; UP000244932; 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   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   Lyase {ECO:0000313|EMBL:SPF30654.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244932};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        84..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          291..582
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   637 AA;  69150 MW;  B3936134172339FF CRC64;
     MSAYDFALPL LQLPRNAKRA IVLSLDALIC IFSVWFALYL RLGELVTLSG PYLIPVFASL
     VIAIPIFVRM GLYRAIYRYS GINSILIIVM ATALYGVLFA TIFTVISVTG VPRTIGIIQP
     ILVMILVVGS RTLARLLLNS YANAEASKGV RVRILIYGAG QTGRQLSAAL AMGGDVKVVG
     FVDDDPRLTG STIDRRPIYS AEDLPDLVKS LDIAHVVLAL PDATRAQMRA VVDRLRDAQV
     SVQTLPDMAA MASGKVTLSD VRPLSIDDLL GRDPVAPDVS LMQQTIKGKS VAITGAGGSI
     GAELCRQICT LEPAQLILIE QSEYSLYAIH QELEAHATRT GISLIPLLGS VTDGQFLSQV
     FAQRSVDTVF HAAAYKHVPL VEQNVAAGIR NNVWGTCVAA EAAAAANVSQ FVLVSTDKAV
     RPTNFMGASK RLAELVLQAF ETRFENTRFS MVRFGNVLGS SGSVVPRFRK QIEEGGPVTL
     THPEITRFFM SIPEAAQLVV QSSAMARGGD VFVLDMGEAV KILDLAERMI ELSGLTIRSD
     EFPEGDIEIQ VTGLRPGEKL YEELLLGDDP QPTRHERIMR AQDACLSWDE LEPKLNELDQ
     ALAANDIETV RRLFVSLPLK YGPNDPIADL LSADPKP
//