ID V9XNX2_9NOCA Unreviewed; 414 AA.
AC V9XNX2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=UDP-glucose/GDP-mannose dehydrogenase {ECO:0000313|EMBL:AHD23047.1};
GN ORFNames=Y013_21645 {ECO:0000313|EMBL:AHD23047.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD23047.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD23047.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD23047.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR EMBL; CP006996; AHD23047.1; -; Genomic_DNA.
DR AlphaFoldDB; V9XNX2; -.
DR KEGG; rpy:Y013_21645; -.
DR PATRIC; fig|1435356.3.peg.4358; -.
DR eggNOG; COG0677; Bacteria.
DR HOGENOM; CLU_023810_3_2_11; -.
DR Proteomes; UP000018781; 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: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; IPR006189; CHASE_dom.
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.
DR PROSITE; PS50839; CHASE; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 12..84
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
SQ SEQUENCE 414 AA; 45571 MW; FE3815A8549B3DCD CRC64;
MAIVGLGYVG LPTALSFHDA GYRVLGLDVN SNRLDTIRRR HVDLIEADRQ RLERAVEDSR
FVLTADPVML RRSTAVAICV PTPVDEHLVP DLGPLMKACK SVVEHTVPGQ LVMLTSTTYV
GCTEELLAAP LRSRGLIPGT DVFVAFSPER INPGTDAYAH ENVPRVVGGV TPACTEAALA
LVAKCVNKVH PVSRAEVAEM SKLLENTFRA VNIALVNEFA DICSHLEIDV TEVVEAAATK
PYGFMPFFPG AGVGGHCIPC DPQYLLWQLR KQRRTAPLIE LSMNEIALRP RHVVERVIRA
LSDRGRRIRG ARVLLVGVAY KPDVEDLRES PALEIMEDLR HEGSVVSYYD PLIPVVRLRD
GTEVESVTDP SAVQPDLVVV HTLHTGEDTN WLADQPQVLD ATYRLKNLPH VLHL
//
