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Database: UniProt
Entry: G9AGW9_RHIFH
LinkDB: G9AGW9_RHIFH
Original site: G9AGW9_RHIFH 
ID   G9AGW9_RHIFH            Unreviewed;       498 AA.
AC   G9AGW9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Nucleotide-sugar dehydrogenase (UDP-glucose/GDP-mannose dehydrogenase) {ECO:0000313|EMBL:CCF00301.1};
DE            EC=1.1.1.- {ECO:0000313|EMBL:CCF00301.1};
GN   OrderedLocusNames=SFHH103_05839 {ECO:0000313|EMBL:CCF00301.1};
OS   Rhizobium fredii (strain HH103) (Sinorhizobium fredii).
OG   Plasmid pSfHH103e {ECO:0000313|EMBL:CCF00301.1,
OG   ECO:0000313|Proteomes:UP000007735}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCF00301.1, ECO:0000313|Proteomes:UP000007735};
RN   [1] {ECO:0000313|EMBL:CCF00301.1, ECO:0000313|Proteomes:UP000007735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HH103 {ECO:0000313|EMBL:CCF00301.1,
RC   ECO:0000313|Proteomes:UP000007735};
RC   PLASMID=pSfHH103e {ECO:0000313|Proteomes:UP000007735};
RX   PubMed=22374952; DOI=10.1128/JB.06729-11;
RA   Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., Margaret I.,
RA   Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., Szczepanowski R.,
RA   Vinardell J.M., Zehner S., Gottfert M.;
RT   "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103.";
RL   J. Bacteriol. 194:1617-1618(2012).
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR   EMBL; HE616899; CCF00301.1; -; Genomic_DNA.
DR   AlphaFoldDB; G9AGW9; -.
DR   KEGG; sfh:SFHH103_05839; -.
DR   PATRIC; fig|380.5.peg.5396; -.
DR   HOGENOM; CLU_023810_3_2_5; -.
DR   Proteomes; UP000007735; Plasmid pSfHH103e.
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   ECO:0000313|EMBL:CCF00301.1}; Plasmid {ECO:0000313|EMBL:CCF00301.1}.
FT   DOMAIN          387..487
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   498 AA;  54408 MW;  14FA4EE8C7DE5447 CRC64;
     MQQFEALQHA SETTHGAVVP RLTWRRFVAN KTEPTRAAAS RKTACSPTNL ETTLTSPHHD
     RLLESISART ARIGVIGLGY VGLPLAIAVA RSGFPVTGFD IDPAKIVALD DGRSYIEAVS
     DDALAREAAA GRFRSTTDFA ELGGCDVIVI CVPTPLTKHR DPDLSFVEKT SRSIAACLRP
     GQFVVLESTT YPGTTDGIVR SILEETGLKS GGDFFLGFSP EREDPGNRNF ETASIPKVVA
     GDGPLAAALM ERFYAAVVET VVPVSSNATA EAVKLTENIF RAVNIALVNE LKVVYEAMGI
     DIWEVIEAAK TKPFGYMPFY PGPGLGGHCI PIDPFYLTWK SREYELPTRF IELAGEINSA
     MPRHVVTRLA EALDLRQGKA LSRSNVLIVG LAYKKNVPDI RESPSLRLIE LIEERGGKAA
     FYDPHVEEIP PTREHMALKG RRSIVFDEKT VRSFDAVLVA TDHDAIDYAA LRDWAPLIID
     TRNVFARRGL AADHVLKA
//
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