ID A0A0F0L7Y3_9MICO Unreviewed; 615 AA.
AC A0A0F0L7Y3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=UDP-N-acetyl-alpha-D-glucosamine C6 dehydratase {ECO:0000313|EMBL:KJL29292.1};
DE EC=4.2.1.135 {ECO:0000313|EMBL:KJL29292.1};
GN Name=pglF {ECO:0000313|EMBL:KJL29292.1};
GN ORFNames=RS83_01921 {ECO:0000313|EMBL:KJL29292.1};
OS Microbacterium oxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=82380 {ECO:0000313|EMBL:KJL29292.1, ECO:0000313|Proteomes:UP000033640};
RN [1] {ECO:0000313|EMBL:KJL29292.1, ECO:0000313|Proteomes:UP000033640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEL4b {ECO:0000313|EMBL:KJL29292.1,
RC ECO:0000313|Proteomes:UP000033640};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL29292.1}.
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DR EMBL; JYIW01000024; KJL29292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0L7Y3; -.
DR PATRIC; fig|82380.11.peg.1957; -.
DR Proteomes; UP000033640; 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:KJL29292.1}; Membrane {ECO:0000256|SAM:Phobius};
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..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 294..571
FT /note="Polysaccharide biosynthesis protein CapD-like"
FT /evidence="ECO:0000259|Pfam:PF02719"
SQ SEQUENCE 615 AA; 66380 MW; 6887E95459357CE6 CRC64;
MPSGSERNEQ VSVWQRRRRI TAAVVDSAAW IFGIVIAVVL RFEFEPTPRG WVSMAVLAVI
AAASQVVVGY YLALYRGRFT YGSFDEVRAL GIAVLVQAAV LSAVVMIVGP FVGLPRGTVI
LAFPFVLLLM FGVRYSARLV IERHRKPGAE AEPALIVGGG YVGDMLLHQM MTDPTSPLRA
VGILDDDPAK KNLRLRGVPV IGRTTEIAAA AEDTGATTLV IAIGGADSML LRRLADDAEQ
AGLRVTITPT LANMMSGEQS ASDLRDISIE DLIGRHPVDT NVELIAGYVT GRRVLVTGAG
GSIGSELCRQ LSKYGPSELI MLDRDETGLQ LAQLGTSGHG LLDSRDVVLA DIRETETLNG
IFADRRPEVV FHAAALKHLP MLEQYPDEAW KTNVLGTLNV LTAAQAVGVD TFVNISTDKA
ANPTSVLGHS KRVAEKLTAW AGEESGMRYL SVRFGNVIGS RGSMLPTFQT LIEAGGPITV
THPDVTRYFM TIPEACQLVI QAGGIGRAGE VLILDMGEPV SILEVAKRMI AMSGKKIEIV
FTGLRHGEKL HEVLVGSTED LERPFHPKVS HTKADSISPD RLDKAGWEAR MLAVPRNNDT
AIIEPIRLDS TEFKK
//
