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Database: UniProt
Entry: A0A2G1Z8C7_9PROT
LinkDB: A0A2G1Z8C7_9PROT
Original site: A0A2G1Z8C7_9PROT 
ID   A0A2G1Z8C7_9PROT        Unreviewed;       436 AA.
AC   A0A2G1Z8C7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   13-SEP-2023, entry version 12.
DE   SubName: Full=UDP-N-acetyl-D-galactosamine dehydrogenase {ECO:0000313|EMBL:PHQ72028.1};
GN   ORFNames=COB93_01575 {ECO:0000313|EMBL:PHQ72028.1};
OS   Sneathiella sp.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sneathiellales;
OC   Sneathiellaceae; Sneathiella.
OX   NCBI_TaxID=1964365 {ECO:0000313|EMBL:PHQ72028.1, ECO:0000313|Proteomes:UP000224255};
RN   [1] {ECO:0000313|Proteomes:UP000224255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-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:PHQ72028.1}.
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DR   EMBL; NVRR01000024; PHQ72028.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G1Z8C7; -.
DR   Proteomes; UP000224255; 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}.
FT   DOMAIN          323..424
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   436 AA;  47013 MW;  09C65B2CDD535DA5 CRC64;
     MAKSIPAALQ EHGEVSSKTK ISVVGLGYVG LPLAIALARG FDVIGYDLNS ERIDELRQGV
     DRTFEIDAPM LRASSVRFTK DIADTRDADI HIITVPTPVD DDSAPDLRPL KTASASIGSI
     MKDGAIVVVE STVYPGVTED VCGPILEEAS GKVSGEGFYL GYSPERINPG DKVHTVDKII
     KVVAGQTDEI TDILADIYGA ATSGGIHRAR NIKTAEAAKV IENAQRDINI AFVNEATMIF
     QKLGVSAYDV LETAGTKWNF LNFTPGLVGG HCIGIDPFYL AHRASEVGYF ADLILTGRRI
     NDSMGTFIAD SIEANLEGKC KILILGLTFK ENVPDLRNTR VVDIITRLRE LGHEVDVHDP
     LANKDEAQKF LNIDLIESLS DLGGYDAIVG AVAHSVYQDL SPAAIEGMMT DTGLVADVKG
     IWRGTEFSSG IKRWLL
//
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