ID A0A1F2PKS5_9FIRM Unreviewed; 590 AA.
AC A0A1F2PKS5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=UDP-N-acetyl-alpha-D-glucosamine C6 dehydratase {ECO:0000313|EMBL:OFV71331.1};
DE EC=4.2.1.135 {ECO:0000313|EMBL:OFV71331.1};
GN Name=pglF_2 {ECO:0000313|EMBL:OFV71331.1};
GN ORFNames=ACWI_12450 {ECO:0000313|EMBL:OFV71331.1};
OS Acetobacterium wieringae.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=52694 {ECO:0000313|EMBL:OFV71331.1, ECO:0000313|Proteomes:UP000176244};
RN [1] {ECO:0000313|EMBL:OFV71331.1, ECO:0000313|Proteomes:UP000176244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1911 {ECO:0000313|EMBL:OFV71331.1,
RC ECO:0000313|Proteomes:UP000176244};
RA Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., Daniel R.;
RT "Genome sequence of Acetobacterium wieringae DSM 1911.";
RL Submitted (SEP-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:OFV71331.1}.
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DR EMBL; LKEU01000024; OFV71331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F2PKS5; -.
DR STRING; 52694.ACWI_12450; -.
DR OrthoDB; 9803111at2; -.
DR Proteomes; UP000176244; 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:OFV71331.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 244..530
FT /note="Polysaccharide biosynthesis protein CapD-like"
FT /evidence="ECO:0000259|Pfam:PF02719"
SQ SEQUENCE 590 AA; 66310 MW; BB44E4AC97A1F260 CRC64;
MSTFLIGGIL VKLIFYLVSG MYNTLWRYAS IEELLQIVIV TFVANAITDI GFKLIGASLP
ASVLVLNLMF DLIFVGMIRV TYRLARRIKI KQISSEAKSE ERVLIFGAGQ AGIAMVKDLM
INSKTKRYNI VGFLDDDPHK ENKKVKGIPI LGNRYAFKEV AKAYDVSQII IACPAVHSKT
IKEVAELANE TQVPVKILPS LDEILNYNVS VSRLRDLQIE DLLNRDEVEL NKDQISSFIR
GKRVMVTGGG GSIGSELCRQ IIRYCPSQMI IVDIYENSLY HLELELNNFL ENNTCIGTTI
DLEIASIRDK KRINDVFESY RPQVVFHAAA HKHVPLMEKT PKEAVKNNIF GTKNLLDAAV
KYQVEKFVQI STDKAVKPTN VMGATKRVCE MLIQTYNKTN QTEFAAVRFG NVLGSNGSVI
PVFKDQIAAG GPVTVTHKDI TRFFMTIPEA TQLVLEAGSI AKGGEIFVLN MGEPVKIIDL
AEKMIRLSGL EPYHDIPIVF SGLRPGEKLY EELSYNLTNF DSTKHEDIFV ENIWPFDKDW
IDQELGRLKH YAETGSDEDV IQQLKSLVPD YLPNRNSPVT IEKVIELEKV
//
