ID K8CVN3_CROSK Unreviewed; 420 AA.
AC K8CVN3;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 ORFNames=BN128_3485 {ECO:0000313|EMBL:CCK09361.1};
OS Cronobacter sakazakii 696.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=1208664 {ECO:0000313|EMBL:CCK09361.1, ECO:0000313|Proteomes:UP000009356};
RN [1] {ECO:0000313|EMBL:CCK09361.1, ECO:0000313|Proteomes:UP000009356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=696 {ECO:0000313|EMBL:CCK09361.1,
RC ECO:0000313|Proteomes:UP000009356};
RX PubMed=23166675; DOI=10.1371/journal.pone.0049455;
RA Joseph S., Desai P., Ji Y., Cummings C.A., Shih R., Degoricija L., Rico A.,
RA Brzoska P., Hamby S.E., Masood N., Hariri S., Sonbol H., Chuzhanova N.,
RA McClelland M., Furtado M.R., Forsythe S.J.;
RT "Comparative analysis of genome sequences covering the seven cronobacter
RT species.";
RL PLoS ONE 7:e49455-e49455(2012).
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: 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:CCK09361.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CALF01000071; CCK09361.1; -; Genomic_DNA.
DR AlphaFoldDB; K8CVN3; -.
DR UniPathway; UPA00566; -.
DR Proteomes; UP000009356; 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}.
FT DOMAIN 324..420
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 126
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 420 AA; 45813 MW; 352ED55F023BD119 CRC64;
MSFNTISVIG LGYIGLPTAA AFASREKQVI GIDINQHAVD TINRGEIHIV EPELDKVVKT
AVEGGFLRAS TTPVEADAYL IAVPTPFKGD HEPDMAYVQA AAESVAPVLR KGALVILEST
SPVGATEQMA QWLAALRPDL SFPQQAGEAA DINIAYCPER VLPGQVMVEL IKNDRVIGGM
TPVCSARASE LYKIFLEGEC VVTNSRTAEM CKLTENSFRD VNIAFANELS LICADQGINV
WELIRLANRH PRVNILQPGP GVGGHCIAVD PWFIVAQNPQ QARLIRTARE VNDHKPHWVI
QQVKSTLADC LAATNRRASE VKIACFGLAF KPNIDDLRES PAMEIAELIA DWHSGETLVV
EPNIHTLPTR LEGKCKLSAL DDALAQADVL VMLVDHQQFK AIDGSTLNHT WVVDTKGVWR
//
