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Database: UniProt
Entry: A0A0B6WZA8_9BACT
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ID   A0A0B6WZA8_9BACT        Unreviewed;       445 AA.
AC   A0A0B6WZA8;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Nucleotide sugar dehydrogenase {ECO:0000313|EMBL:CDM66578.1};
DE            EC=1.1.1.136 {ECO:0000313|EMBL:CDM66578.1};
GN   ORFNames=PYK22_02610 {ECO:0000313|EMBL:CDM66578.1};
OS   Pyrinomonas methylaliphatogenes.
OC   Bacteria; Acidobacteriota; Blastocatellia; Blastocatellales;
OC   Pyrinomonadaceae; Pyrinomonas.
OX   NCBI_TaxID=454194 {ECO:0000313|EMBL:CDM66578.1, ECO:0000313|Proteomes:UP000031518};
RN   [1] {ECO:0000313|EMBL:CDM66578.1, ECO:0000313|Proteomes:UP000031518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K22 {ECO:0000313|EMBL:CDM66578.1,
RC   ECO:0000313|Proteomes:UP000031518};
RA   Stott M.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDM66578.1, ECO:0000313|Proteomes:UP000031518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K22 {ECO:0000313|EMBL:CDM66578.1,
RC   ECO:0000313|Proteomes:UP000031518};
RA   Lee K.C.Y., Power J.F., Dunfield P.F., Morgan X.C., Huttenhower C.,
RA   Stott M.B.;
RT   "Complete genome sequence of Pyrinomonas methylaliphatogenes type strain
RT   K22T.";
RL   Submitted (JAN-2015) 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; CBXV010000008; CDM66578.1; -; Genomic_DNA.
DR   RefSeq; WP_041977933.1; NZ_CBXV010000008.1.
DR   AlphaFoldDB; A0A0B6WZA8; -.
DR   STRING; 454194.PYK22_02610; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000031518; 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:0047004; F:UDP-N-acetylglucosamine 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   ECO:0000313|EMBL:CDM66578.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031518}.
FT   DOMAIN          330..432
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   445 AA;  48936 MW;  8E3452D8D8E47F25 CRC64;
     MIKESLIDLI EKKRAHIGVI GLGYVGLPLA VEFARKGFRA TGFEVDGRKV ERIKSGDSYI
     GDVPSSALKE AVTAQRLDAT TDFKLLRDCD CIIICVPTPL RKTKEPDISY ILAATEEIKK
     SLRRGQLIVL ESTTYPGTTD EVLLPAFEET GLKLDQDFLL AFSPERVDPG NPKYQTHNIP
     KVVGGVSPAS TEAAAALYGQ IVNEVHPVSS ARVAEAAKLL ENTFRAVNIG MANEMARLCY
     ALGIDTWEVI RAAATKPFGF MPFYPGPGIG GHCIPLDPHY LSWKARQHGF ESRFISLAEE
     VNSRMPEHVV QLVIDGLNDD RKALKGARIL LLGVAYKKDV DDVRESPALS IIDRLRAKGA
     DVRYHDPHVE EVRFDDAHTQ AGGDPLRSVA LTPEELAAAD CVVIVTDHSK VDYEMVVEHA
     RLIVDTRNAL NGDLRQTAKA RIIRL
//
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