ID A0A1V4I5R1_9FIRM Unreviewed; 610 AA.
AC A0A1V4I5R1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=UDP-N-acetyl-alpha-D-glucosamine C6 dehydratase {ECO:0000313|EMBL:OPJ55321.1};
DE EC=4.2.1.135 {ECO:0000313|EMBL:OPJ55321.1};
GN Name=pglF {ECO:0000313|EMBL:OPJ55321.1};
GN ORFNames=CLOTH_16240 {ECO:0000313|EMBL:OPJ55321.1};
OS [Clostridium] thermoalcaliphilum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX NCBI_TaxID=29349 {ECO:0000313|EMBL:OPJ55321.1, ECO:0000313|Proteomes:UP000190140};
RN [1] {ECO:0000313|EMBL:OPJ55321.1, ECO:0000313|Proteomes:UP000190140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7309 {ECO:0000313|EMBL:OPJ55321.1,
RC ECO:0000313|Proteomes:UP000190140};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium thermoalcaliphilum DSM 7309.";
RL Submitted (MAR-2017) 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:OPJ55321.1}.
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DR EMBL; MZGW01000006; OPJ55321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4I5R1; -.
DR STRING; 29349.CLOTH_16240; -.
DR OrthoDB; 9803111at2; -.
DR Proteomes; UP000190140; 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 Coiled coil {ECO:0000256|SAM:Coils}; Lyase {ECO:0000313|EMBL:OPJ55321.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000190140};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 282..565
FT /note="Polysaccharide biosynthesis protein CapD-like"
FT /evidence="ECO:0000259|Pfam:PF02719"
FT COILED 572..599
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 610 AA; 68655 MW; 9598BA15CDF5BAEC CRC64;
MNKIRFRQGI LLILDIILVN IAAILSLELI FNFNTSVQYV TFLKQSSIIY TFIIIATFYI
FKCYKSLWRY ASIEEMISII ISSVLSMIAI YNVFHFTKAT LPINFYILNT LMLIGLTGGL
RFSYRAIRKL KIKYSLKNGS RVLIIGGGVA GALVIKELFN NPQIKKFPVG IIDDDNTKLG
RAIHGVPVLG DRQRIKEIVG KKKVDEIIIA IPSMSKSEKS KLIEMCKETK CKLKTLPGMY
EIIDGRVDIK NIRDVDIEDL LGREPIKVNL EEISDYIQNE VVLVTGGGGS IGSELCRQIA
RFNPKELILL DIYENNAYEI QQELIRKYKD KLNLKVIIAS VRDKKRMEQI FIDYNPKVVF
HAAAHKHVPL MEDSPTEAVK NNVFGTLNVA ELSDKYNIKR FVLISTDKAV NPTNIMGATK
RMAEIIIQTL NKHSDTEFVA VRFGNVLGSN GSVIPLFKKQ IAEGGPVTIT HPDIIRYFMT
IPEAVQLVIQ AGAMAKGGEI FVLDMGDPVK ITNLAKDLIK LSGLEPDVDI EIKFTGLRPG
EKLYEELLMA EEGLTGTKHK KIFVGKPIDI DVKALYNELE ILQNVVRNEE NELVDIVIKK
MVPTYTKSVS
//