ID A0A386HRD0_9BACT Unreviewed; 434 AA.
AC A0A386HRD0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Nucleotide sugar dehydrogenase {ECO:0000313|EMBL:AYD47991.1};
GN ORFNames=D6B99_10555 {ECO:0000313|EMBL:AYD47991.1};
OS Arachidicoccus soli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Arachidicoccus.
OX NCBI_TaxID=2341117 {ECO:0000313|EMBL:AYD47991.1, ECO:0000313|Proteomes:UP000266118};
RN [1] {ECO:0000313|EMBL:AYD47991.1, ECO:0000313|Proteomes:UP000266118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIS59-12 {ECO:0000313|EMBL:AYD47991.1,
RC ECO:0000313|Proteomes:UP000266118};
RA Weon H.-Y., Kwon S.-W., Lee S.A.;
RT "Arachidicoccus sp. nov., a bacterium isolated from soil.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR EMBL; CP032489; AYD47991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A386HRD0; -.
DR KEGG; ark:D6B99_10555; -.
DR OrthoDB; 9803238at2; -.
DR Proteomes; UP000266118; 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:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
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:SF2; 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:UP000266118}.
FT DOMAIN 329..427
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 434 AA; 48009 MW; F65FA5ACCBF53F49 CRC64;
MPTPQNKKIA IIGLGYVGLP LAIEFAAHFP VIGFDISKDR VEELNAGKDR TQEADLEKLN
RHLQVAKNND FASGLICSND LEVLKTANIF IVTVPTPIDK YNSPDLTPLL KASEMLGKVI
KQGDTIIYES TVYPGCTEED CVPVLEKFSN LKFNRDFFVG YSPERINPGD KVHTLTSVKK
VTSGSTPAIA EEVNNLYKTI ITAGTHLAPS IKVAEASKAI ENAQRDVNIS FVNELALIFD
RVGIDTNDVL DAAGTKYNFL KYKPGLVGGH CISVDPYYLA HKATQLGYHP QVILSGRRVN
DMMAAFIAGK VVKLMIQKGH TAIKGAKALI LGVTFKENCP DVRNTKVVDI YKELQQFGLE
VDIYDPWADK SEVKHEYGVN IIASLENQTD YAALIIAVAH EEFKTINYRE YKDKNAVIFD
AKAFVDRNLV DGRL
//
