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Database: UniProt
Entry: D3A0K7_NEIMU
LinkDB: D3A0K7_NEIMU
Original site: D3A0K7_NEIMU 
ID   D3A0K7_NEIMU            Unreviewed;       439 AA.
AC   D3A0K7;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Nucleotide sugar dehydrogenase {ECO:0000313|EMBL:EFC87137.1};
GN   ORFNames=NEIMUCOT_06443 {ECO:0000313|EMBL:EFC87137.1};
OS   Neisseria mucosa ATCC 25996.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=546266 {ECO:0000313|EMBL:EFC87137.1, ECO:0000313|Proteomes:UP000003344};
RN   [1] {ECO:0000313|EMBL:EFC87137.1, ECO:0000313|Proteomes:UP000003344}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25996 {ECO:0000313|EMBL:EFC87137.1,
RC   ECO:0000313|Proteomes:UP000003344};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2009) 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:EFC87137.1}.
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DR   EMBL; ACDX02000029; EFC87137.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3A0K7; -.
DR   STRING; 546266.NEIMUCOT_06443; -.
DR   eggNOG; COG0677; Bacteria.
DR   Proteomes; UP000003344; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003344};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          332..431
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   439 AA;  48616 MW;  CC9049A853C0BEA5 CRC64;
     MRPIMKNTTI QKFADKTAKI GIVGLGYVGL PLMLRYVDIG YQVLGFDIDK TKVDKLNKGE
     TYIEHIPAEK IAAASNSLFE ATTDFSRIGE VEAVILCVPT PLNKYREPDM SFVIDTTDAV
     KPYLRAGQVL SLESTTYPGT TEEELLPRVE EGGLKVGKDV FLVYSPERED PGNPNFETRT
     IPKVIGGHTP ACLEVGIALY QPAIDKVVPV SSTKAAELTK LLENIHRAVN IGLVNEMKIV
     ADKMDVDIHE VIAAAATKPF GFVAYYPGPG LGGHCIPIDP FYLTWKAREY GVNTRFIELA
     GEVNSHMPDY VIGKVGLALN EHNRSIKDSK ILVLGIAYKK NVDDMRESPS VEVMDRLHKL
     GANISYSDPH VLEFPYIPGH HYFDLKSEPL TPETVAKYDC VVLTTDHDKF DYDMIAEHAK
     LIVDTRGKFP AKNPKVVKA
//
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