ID S6HQ77_9GAMM Unreviewed; 424 AA.
AC S6HQ77;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=VI polysaccharide biosynthesis protein VipA/TviB family protein {ECO:0000313|EMBL:EPJ54057.1};
GN ORFNames=OFPI_08030 {ECO:0000313|EMBL:EPJ54057.1};
OS Osedax symbiont Rs2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae.
OX NCBI_TaxID=1330035 {ECO:0000313|EMBL:EPJ54057.1, ECO:0000313|Proteomes:UP000014830};
RN [1] {ECO:0000313|EMBL:EPJ54057.1, ECO:0000313|Proteomes:UP000014830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs2 {ECO:0000313|Proteomes:UP000014830};
RA Yi H., Goffredi S.;
RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT Osedax worms: functional variation and environmental selection.";
RL Submitted (MAY-2013) 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:EPJ54057.1}.
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DR EMBL; ASZI01000052; EPJ54057.1; -; Genomic_DNA.
DR AlphaFoldDB; S6HQ77; -.
DR PATRIC; fig|1330035.3.peg.766; -.
DR Proteomes; UP000014830; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000014830}.
FT DOMAIN 318..417
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 424 AA; 46694 MW; ECE9F20938B15245 CRC64;
MRDLNELKIA IIGLGYVGLP LAIEFGKNYS VVGFDVNVKR ISDLAAGVDA TLEVSDEELK
SAENLSFTAD YHQLEECNFY IVTVPTPIDS SNQPDLRPLK AASEMLSKVI TENDVVVYES
TVYPGTTEEI CVPILQAGSG LGYNSDLFIG YSPERINPGD KIHRVSTIKK VTSGSNPDTA
SYVDQVYNLV ITAGTHLAPS IKVAEASKVI ENTQRDVNIA LINELAIIFN KLEIDTLEVL
EAAGSKWNFL PFRPGLVGGH CISVDPYYLT HKAQSVGYHP AMILAGRRLN DGMGQYVASQ
LVKAMLKKKI QVQGAKVLIM GFAFKENCPD LRNTKVIDIV RELADYGAEV DVCDPWCSSE
EAQQVYELQL IEPMVDQYDA IVIAVAHQQY FEMGGGAIHS LGKSNHVLYD LKYVLEKKEV
DLRL
//
