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Database: UniProt
Entry: A0A1Q4GQ51_9PROT
LinkDB: A0A1Q4GQ51_9PROT
Original site: A0A1Q4GQ51_9PROT 
ID   A0A1Q4GQ51_9PROT        Unreviewed;       426 AA.
AC   A0A1Q4GQ51;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=GDP-mannose dehydrogenase {ECO:0000313|EMBL:OJZ17576.1};
GN   ORFNames=BGP21_05550 {ECO:0000313|EMBL:OJZ17576.1};
OS   Thiobacillus sp. 65-29.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=1895862 {ECO:0000313|EMBL:OJZ17576.1, ECO:0000313|Proteomes:UP000186483};
RN   [1] {ECO:0000313|EMBL:OJZ17576.1, ECO:0000313|Proteomes:UP000186483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=65-29 {ECO:0000313|EMBL:OJZ17576.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000124}.
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:OJZ17576.1}.
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DR   EMBL; MKWN01000043; OJZ17576.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q4GQ51; -.
DR   STRING; 1895862.BGP21_05550; -.
DR   Proteomes; UP000186483; Unassembled WGS sequence.
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}.
FT   DOMAIN          313..413
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   426 AA;  46321 MW;  BD786CD15FE9C643 CRC64;
     MSVVAVVGLG YVGLPLAAEF GKKTTTIGYD LSAEKIESYR RFCDPTGEVS TDDLRAATQL
     TVTTDPADLA QADFIIVAVP TPVDDAHIPD FSPLVGSSTT VGKYMKKGAT VIYESTVYPG
     ATEEVCIPLL EKHSGMKWRQ DFHVGYSPER VNPGDRERTI TKITKVVSGD DAATLEKVAT
     LYESVITAGV HRASSIKVAE AAKVIENTQR DLNIALMNEL SLIFHRLGID TLEVLKAAGT
     KWNFLPFRPG LVGGHCIGVD PYYLTHKADM LGYHPQVILA GRRINDGMGA YVAQETVKKM
     IANGVPVKGA RVNVLGLTFK ENCPDLRNSK VVDVIRELQS FGCDVHVHDP LGESREAEHE
     YGITLTPWED LPECDAMIAA VSHAAYLEKP FSELAAKLKK GGVFTDVKSA YDPVMVKAAG
     FALWRL
//
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