ID Q8PXR2_METMA Unreviewed; 478 AA.
AC Q8PXR2;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=UDP-N-acetyl-D-mannosamine dehydrogenase {ECO:0000256|ARBA:ARBA00016796};
DE EC=1.1.1.336 {ECO:0000256|ARBA:ARBA00012935};
DE AltName: Full=UDP-ManNAc 6-dehydrogenase {ECO:0000256|ARBA:ARBA00030172};
GN OrderedLocusNames=MM_1154 {ECO:0000313|EMBL:AAM30850.1};
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952 {ECO:0000313|EMBL:AAM30850.1, ECO:0000313|Proteomes:UP000000595};
RN [1] {ECO:0000313|EMBL:AAM30850.1, ECO:0000313|Proteomes:UP000000595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
RC {ECO:0000313|Proteomes:UP000000595};
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baumer S., Jacobi C.,
RA Bruggemann H., Lienard T., Christmann A., Bomeke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.P., Gunsalus R.P.,
RA Fritz H.J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2] {ECO:0007829|PDB:3G79}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 3-469.
RA Malashkevich V.N., Sauder J.M., Burley S.K., Almo S.C.;
RT "Crystal structure of NDP-N-acetyl-D-galactosaminuronic acid dehydrogenase
RT from Methanosarcina mazei Go1.";
RL Submitted (FEB-2009) to the PDB data bank.
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|ARBA:ARBA00001205};
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR EMBL; AE008384; AAM30850.1; -; Genomic_DNA.
DR PDB; 3G79; X-ray; 2.40 A; A/B=3-469.
DR PDBsum; 3G79; -.
DR AlphaFoldDB; Q8PXR2; -.
DR SMR; Q8PXR2; -.
DR KEGG; mma:MM_1154; -.
DR PATRIC; fig|192952.21.peg.1352; -.
DR eggNOG; arCOG00252; Archaea.
DR HOGENOM; CLU_023810_3_2_2; -.
DR EvolutionaryTrace; Q8PXR2; -.
DR Proteomes; UP000000595; Chromosome.
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:0089714; F:UDP-N-acetyl-D-mannosamine dehydrogenase activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3G79}; Membrane {ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AAM30850.1}; 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 356..454
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 478 AA; 51826 MW; 65BC245EFB4FF4B9 CRC64;
MISMSKLEKL LKERGPIKKI GVLGMGYVGI PAAVLFADAP CFEKVLGFQR NSKSSGYKIE
MLNRGESPLK GEEPGLEELI GKVVKAGKFE CTPDFSRISE LDAVTLAIQT PFANPKDLEP
DFSALIDGIR NVGKYLKPGM LVVLESTITP GTTEGMAKQI LEEESGLKAG EDFALAHAPE
RVMVGRLLKN IREHDRIVGG IDEASTKRAV ELYSPVLTVG QVIPMSATAA EVTKTAENTF
RDLQIAAINQ LALYCEAMGI NVYDVRTGVD SLKGEGITRA VLWPGAGVGG HCLTKDTYHL
ERGVKIGRGE LDYPEGADSI YVLARKVNDF MPAHMYNLTV AALERLGKKM DGSKVAMLGW
AFIKDSDDAR NTPSEPYRDL CLKAGASVMV HDPYVVNYPG VEISDNLEEV VRNADAIVVL
AGHSAYSSLK ADWAKKVSAK ANPVIIDGRN VIEPDEFIGK GFVYKGIGRG DKNSHKIK
//
