ID A0A1E7Z1S6_9GAMM Unreviewed; 430 AA.
AC A0A1E7Z1S6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=UDP-N-acetyl-D-mannosamine dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02029};
DE EC=1.1.1.336 {ECO:0000256|HAMAP-Rule:MF_02029};
DE AltName: Full=UDP-ManNAc 6-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02029};
GN Name=wecC {ECO:0000256|HAMAP-Rule:MF_02029,
GN ECO:0000313|EMBL:OFC62709.1};
GN ORFNames=ACZ87_00425 {ECO:0000313|EMBL:RAP72745.1}, BBW68_08495
GN {ECO:0000313|EMBL:OFC62709.1};
OS Candidatus Erwinia dacicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=252393 {ECO:0000313|EMBL:OFC62709.1, ECO:0000313|Proteomes:UP000243534};
RN [1] {ECO:0000313|EMBL:OFC62709.1, ECO:0000313|Proteomes:UP000243534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL {ECO:0000313|EMBL:OFC62709.1,
RC ECO:0000313|Proteomes:UP000243534};
RA Yuval B.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RAP72745.1, ECO:0000313|Proteomes:UP000244334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oroville {ECO:0000313|EMBL:RAP72745.1,
RC ECO:0000313|Proteomes:UP000244334};
RA Estes A.M., Hearn D.J., Agarwal S., Pierson E.A., Dunning-Hotopp J.C.;
RT "Genomes of the Obligate Erwinia dacicola and Facultative Enterobacter sp.
RT OLF Endosymbionts of the Olive Fruit fly, Bactrocera oleae.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the four-electron oxidation of UDP-N-acetyl-D-
CC mannosamine (UDP-ManNAc), reducing NAD(+) and releasing UDP-N-
CC acetylmannosaminuronic acid (UDP-ManNAcA). {ECO:0000256|HAMAP-
CC Rule:MF_02029}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + 2 NAD(+) + UDP-N-acetyl-alpha-D-mannosamine = 3 H(+) + 2
CC NADH + UDP-N-acetyl-alpha-D-mannosaminouronate; Xref=Rhea:RHEA:25780,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:68623, ChEBI:CHEBI:70731;
CC EC=1.1.1.336; Evidence={ECO:0000256|HAMAP-Rule:MF_02029};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02029}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02029}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. WecC subfamily. {ECO:0000256|HAMAP-Rule:MF_02029}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02029}.
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:OFC62709.1}.
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DR EMBL; MAYS01000197; OFC62709.1; -; Genomic_DNA.
DR EMBL; LJAM02000015; RAP72745.1; -; Genomic_DNA.
DR RefSeq; WP_070134451.1; NZ_MAYS01000197.1.
DR AlphaFoldDB; A0A1E7Z1S6; -.
DR OrthoDB; 9803238at2; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000243534; Unassembled WGS sequence.
DR Proteomes; UP000244334; 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:0089714; F:UDP-N-acetyl-D-mannosamine dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR HAMAP; MF_02029; WecC_RffD; 1.
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 InterPro; IPR032891; WecC.
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, ECO:0000256|HAMAP-Rule:MF_02029};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02029}; Reference proteome {ECO:0000313|Proteomes:UP000244334}.
FT DOMAIN 324..421
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT ACT_SITE 212
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 160
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 161
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 212
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 216
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 219
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 250
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 252
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 263
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 330
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 331
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 338
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
FT BINDING 416
FT /ligand="UDP-N-acetyl-alpha-D-mannosaminouronate"
FT /ligand_id="ChEBI:CHEBI:70731"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02029"
SQ SEQUENCE 430 AA; 47330 MW; EC966074B0CD60DD CRC64;
MSFNTISVIG LGYIGLPTAA AFASRQKQVL GIDINAHAVE TINRGDIHIV EPDLDRVVKT
AVDGGYLRAA TQPQAADAFL IAVPTPFKGE HQPDMAYVQA AAETIASVLK KGDLVILEST
SPVGASEQMA AWLATARPDL SFPHQAGEQA DIQVAYCPER VLPGQVMVEL FKNDRVIGGM
TTVCSQRACD LYNIFLEGEC VVTNSRTAEM CKLTENSFRD VNIAFANELS LICAEQDINV
WELIRLANRH PRVNILQPGP GVGGHCIAVD PWFIVAQNPE QARLIRMARE VNDGKPHWVL
EQVQRQVADC LMRSNKRASE LKIACLGLTF KPDIDDLRES PAVQVTKLIA DWHQGSTLVV
EPNVQQLPAK LQQSVTLVAL DDALQQADVL VLLVDHRQFK TIDPASVNQP WIVDTKGVWR
MRYSSCERDT
//
