ID Q5L7I1_BACFN Unreviewed; 400 AA.
AC Q5L7I1;
DT 21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 21-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=UDP-N-acetyl-D-mannosamine dehydrogenase {ECO:0000313|EMBL:CAH09971.1};
GN ORFNames=BF9343_4190 {ECO:0000313|EMBL:CAH09971.1};
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH09971.1, ECO:0000313|Proteomes:UP000006731};
RN [1] {ECO:0000313|EMBL:CAH09971.1, ECO:0000313|Proteomes:UP000006731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC Onslow {ECO:0000313|Proteomes:UP000006731};
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR EMBL; CR626927; CAH09971.1; -; Genomic_DNA.
DR RefSeq; WP_005791918.1; NZ_UFTH01000001.1.
DR PaxDb; 272559-BF9343_4190; -.
DR GeneID; 66330929; -.
DR KEGG; bfs:BF9343_4190; -.
DR eggNOG; COG0677; Bacteria.
DR HOGENOM; CLU_023810_3_2_10; -.
DR BioCyc; BFRA272559:G1GHZ-4634-MONOMER; -.
DR Proteomes; UP000006731; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017476; UDP-Glc/GDP-Man.
DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR InterPro; IPR036220; UDP-Glc/GDP-Man_DH_C_sf.
DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR InterPro; IPR028359; UDP_ManNAc/GlcNAc_DH.
DR NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR PANTHER; PTHR43491; UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE; 1.
DR PANTHER; PTHR43491:SF1; UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE; 1.
DR Pfam; PF00984; UDPG_MGDP_dh; 1.
DR Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR Pfam; PF03721; UDPG_MGDP_dh_N; 1.
DR PIRSF; PIRSF500136; UDP_ManNAc_DH; 1.
DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006731};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..400
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041118621"
FT DOMAIN 311..400
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 400 AA; 44819 MW; 003F82AB3DD7671D CRC64;
MKKVVFLGLG YIGLPTAAVA AGHGYEVVGV DVNPSVVETI NQGKIHIVEP ELDQIVKEVV
RTGNLRAVSK PEQADAFFVV VPTPFKQNHR ADITYVESAT RSVIPYLREG NLFVIESTSP
VFTTERMAEV IYKERPELKD KIYIAYCPER VLPGNTLYEL VHNDRVIGGV NPESTAKAIE
FYSAFVQGKL HPTNARTAEM CKLTENSSRD SQIAFANELS MICDKAGINV WELIELANKH
PRVNILQPGC GVGGHCIAVD PWFIVSDYPE QAQIIKRARE TNDYKADWCA NKVMEACQQF
VEKNDREPVV ACMGLAFKPN IDDLRESPAK YIASRIVSES RAEVLIVEPN VASHASFHLT
DYREAYQKAD IVVWLVRHTP FVELPREESK LELDFCGVRK
//
