ID A0A2N3Y470_SACSN Unreviewed; 448 AA.
AC A0A2N3Y470;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Nucleotide sugar dehydrogenase {ECO:0000313|EMBL:PKW17729.1};
GN ORFNames=A8926_5732 {ECO:0000313|EMBL:PKW17729.1};
OS Saccharopolyspora spinosa.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=60894 {ECO:0000313|EMBL:PKW17729.1, ECO:0000313|Proteomes:UP000233786};
RN [1] {ECO:0000313|EMBL:PKW17729.1, ECO:0000313|Proteomes:UP000233786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44228 {ECO:0000313|EMBL:PKW17729.1,
RC ECO:0000313|Proteomes:UP000233786};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 Actinobacteria strains.";
RL Submitted (DEC-2017) 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:PKW17729.1}.
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DR EMBL; PJNB01000001; PKW17729.1; -; Genomic_DNA.
DR RefSeq; WP_010311564.1; NZ_PJNB01000001.1.
DR AlphaFoldDB; A0A2N3Y470; -.
DR STRING; 994479.GCA_000194155_05568; -.
DR OrthoDB; 5193947at2; -.
DR Proteomes; UP000233786; 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}.
FT DOMAIN 348..441
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 448 AA; 48284 MW; 4312CB83525CF35A CRC64;
MTEHPLALAV NGRERLLADR LIAFEPRMPE RTESVVVVGL GYVGLPTACA LQSPTAQVIG
FDISEDRLQA IKAGEVDMPE LERRALTASL AAGDLQLSCD PSVLAGADAV IVCVPTPVDT
AHQPDLTALR AACETVVAFA RRGQTIILTS TTFAGTTRQL LVEPLEQRGM RVGTDVHVAF
SPERIDPGNF DHVQRETPRV VGGVTPRCAD RAAEVVSRMT DSVYLVSSPE AAELTKLYEN
IFRAVNLALA NEMADACSVL GLDPIEVTIA AGTKPYGFLG SFPGPGVGGH CIPCDPYYLL
WQLRREGVSA PVIEQAMRSI DQRPGQVVQR VVEMLGDAGI DHSGARVVVA GVSYKAGVRD
LRESPALPIL AGLRRIGIAV HYFDPLLPEI TLADGTRMVS EPAPRGRDWD VTVLHTLHPG
VDYGWARDCP QVLDATYQFD AVPHRRVL
//
