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Database: UniProt
Entry: A0A1M4NBN9_9CLOT
LinkDB: A0A1M4NBN9_9CLOT
Original site: A0A1M4NBN9_9CLOT 
ID   A0A1M4NBN9_9CLOT        Unreviewed;       617 AA.
AC   A0A1M4NBN9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=UDP-N-acetyl-alpha-D-glucosamine C6 dehydratase {ECO:0000313|EMBL:SCN23792.1};
DE            EC=4.2.1.135 {ECO:0000313|EMBL:SCN23792.1};
GN   Name=pglF {ECO:0000313|EMBL:SCN23792.1};
GN   ORFNames=N3C_1498 {ECO:0000313|EMBL:SCN23792.1};
OS   Clostridium sp. N3C.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1776758 {ECO:0000313|EMBL:SCN23792.1, ECO:0000313|Proteomes:UP000184869};
RN   [1] {ECO:0000313|EMBL:SCN23792.1, ECO:0000313|Proteomes:UP000184869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N3C {ECO:0000313|EMBL:SCN23792.1};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) 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; FMJL01000019; SCN23792.1; -; Genomic_DNA.
DR   RefSeq; WP_074365418.1; NZ_FMJL01000019.1.
DR   AlphaFoldDB; A0A1M4NBN9; -.
DR   STRING; 1776758.N3C_1498; -.
DR   OrthoDB; 9803111at2; -.
DR   Proteomes; UP000184869; 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:SCN23792.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184869};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        39..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        108..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          291..573
FT                   /note="Polysaccharide biosynthesis protein CapD-like"
FT                   /evidence="ECO:0000259|Pfam:PF02719"
SQ   SEQUENCE   617 AA;  70278 MW;  ED28C1B423D0AA39 CRC64;
     MRKINKLIII DIVFVILSLY LAFLLRFDFG MDNAYKEYLN FAMMSIVPFV IITIACNYLF
     SLYSRIWRYA SVEELLSIVL SVSLSNVLFI VYSYVINYKV LHTSYFRFPF SMHIIAWIIS
     VALLGGVRFI FRIGDAANQF KEGTTGKKKL LIIGAGEAAA MLIREIKNHR ELNYNIIGLI
     DDDVSKLGRK IKGVKVLGDR SDIEKVCKEY KVDEIIVAIP SADNKTKREI YNKCKNTKCK
     LKTLPGIYEL IDNKKIEISK IRDVNIEDLL GREEVHLNIE GISKYVKDKV VLVTGGGGSI
     GSELCRQVAK FDPSKLLVLD IYENGAYDLQ MQLKYDYPDL DLEVVIASIR DYERLKQLFE
     QYKPDVVFHA AAHKHVPLME DNPSEAIKNN ILGTYNLLNC ARDYKVKKFV QISTDKAVNP
     TNIMGATKRF CEIMVQAFDK VSETEFVAVR FGNVLGSNGS VIPLFKEQIA KGGPVTVTHP
     EINRFFMTIP EAAQLVLQAG AMADGGEIFV LDMGKPVKIV DLARDLIRLS GLKPDEDIKI
     KYTGLRKGEK LYEELLMSEV ALTSTNHEKI FVEKPMEYDM EFVKQSVEEF QNIIYSDKEE
     IFKLIQKKVP TYKRNLN
//
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