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Database: UniProt
Entry: A3WFB6_9SPHN
LinkDB: A3WFB6_9SPHN
Original site: A3WFB6_9SPHN 
ID   A3WFB6_9SPHN            Unreviewed;       434 AA.
AC   A3WFB6;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   SubName: Full=UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase {ECO:0000313|EMBL:EAQ28203.1};
GN   ORFNames=NAP1_11428 {ECO:0000313|EMBL:EAQ28203.1};
OS   Erythrobacter sp. NAP1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=237727 {ECO:0000313|EMBL:EAQ28203.1, ECO:0000313|Proteomes:UP000002995};
RN   [1] {ECO:0000313|EMBL:EAQ28203.1, ECO:0000313|Proteomes:UP000002995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAP1 {ECO:0000313|EMBL:EAQ28203.1,
RC   ECO:0000313|Proteomes:UP000002995};
RX   PubMed=21952547; DOI=10.1128/JB.05845-11;
RA   Koblizek M., Janouskovec J., Obornik M., Johnson J.H., Ferriera S.,
RA   Falkowski P.G.;
RT   "Genome Sequence of the Marine Photoheterotrophic Bacterium Erythrobacter
RT   sp. Strain NAP1.";
RL   J. Bacteriol. 193:5881-5882(2011).
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:EAQ28203.1}.
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DR   EMBL; AAMW01000002; EAQ28203.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3WFB6; -.
DR   STRING; 237727.NAP1_11428; -.
DR   eggNOG; COG0677; Bacteria.
DR   HOGENOM; CLU_023810_3_2_5; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000002995; 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: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:UP000002995}.
FT   DOMAIN          336..434
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   434 AA;  46504 MW;  A77B22B6CB3D3F7D CRC64;
     MNAPFDTASA IGPDAAIQPA PDHQVVVVGL GYIGLPTAAV LASHGWNVCG VDVSEKVVET
     VNAGRVHIEE RDLDRLVREA TESERLTAST QVPTAHFYMI AVPTPLTDEK TPDISYVEAA
     ARAIAPKILP GACVIVESTS PVGTTERVGQ IIAEMRPDLQ VPVYGSQQGG DIALAYCPER
     VLPGKIVREL VQNDRVIGGI TPYCAERAAA LYSSFVEGDC LTTNVRVAET VKLTENSYRD
     VNIAFANELS VIADDLGVDV WDVISLANRH PRVNILQPGP GVGGHCIAVD PWFLVSSSPK
     AARLIRTARE VNDFKATYTE RRVRALLDAV PGGKVALLGL AFKPDIDDFR ESPALEIALS
     LAKTRGQRIM VVEPFADELP KGFAGTGAQL VKLDEALATA EVIVVLVDHT AFKHLLPADL
     AGKLVFDTRG MLKK
//
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