ID B8FWK7_DESHD Unreviewed; 451 AA.
AC B8FWK7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Nucleotide sugar dehydrogenase {ECO:0000313|EMBL:ACL22505.1};
DE EC=1.1.1.22 {ECO:0000313|EMBL:ACL22505.1};
GN OrderedLocusNames=Dhaf_4504 {ECO:0000313|EMBL:ACL22505.1};
OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564 {ECO:0000313|EMBL:ACL22505.1, ECO:0000313|Proteomes:UP000007726};
RN [1] {ECO:0000313|EMBL:ACL22505.1, ECO:0000313|Proteomes:UP000007726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10664 / DCB-2 {ECO:0000313|Proteomes:UP000007726};
RX PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA Tiedje J.M.;
RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT anaerobe capable of dehalogenation and metal reduction.";
RL BMC Microbiol. 12:21-21(2012).
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR EMBL; CP001336; ACL22505.1; -; Genomic_DNA.
DR RefSeq; WP_011461043.1; NC_011830.1.
DR AlphaFoldDB; B8FWK7; -.
DR KEGG; dhd:Dhaf_4504; -.
DR HOGENOM; CLU_023810_3_2_9; -.
DR Proteomes; UP000007726; 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 ECO:0000313|EMBL:ACL22505.1}.
FT DOMAIN 342..440
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 451 AA; 49569 MW; 15FDECD4AE69F95E CRC64;
MLRMKEVITS EDVLAKNLKD KLQDHSATVG VIGLGYVGLP LAVEKGKVGF SVIGFDINAA
RVAKVNAGDN YIADVKDEEL LELTQKGMIT ATTDYAKLAE CDVVVICVPT PLTITRDPDI
SYIQASSEQI AKYLKPGQLV TLESTTYPGT TEEVILPMLE QSGLKVGKDF FLAFSPERVD
PGNKRFTTNN TSKVVGGMTP VCLEVAYTFY AQTIVNVVPV SSPAAAELTK VFENTYRAVN
IALVNELMLL CDRMGIDIWE VVEAAGTKPF GIQTFWPGPG VGGHCIPIDP FYLTWKAREY
DFHTRFIELA GEINVEVSYH VINKVIRALN NENKSLKDAK VLILGVAYKK DIDDVRESPA
LKIMELLRKN GANIAYHDPY IPVIEPHGGS TVHLENTELT DEALAAADCV LILTDHSVVD
YERVAEKAPL IVDTRNATRG VENNREKIVK I
//
