ID G7VDG9_9CREN Unreviewed; 461 AA.
AC G7VDG9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ORFNames=P186_1325 {ECO:0000313|EMBL:AET32754.1};
OS Pyrobaculum ferrireducens.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=1104324 {ECO:0000313|EMBL:AET32754.1, ECO:0000313|Proteomes:UP000005867};
RN [1] {ECO:0000313|EMBL:AET32754.1, ECO:0000313|Proteomes:UP000005867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1860 {ECO:0000313|EMBL:AET32754.1,
RC ECO:0000313|Proteomes:UP000005867};
RX PubMed=22247528; DOI=10.1128/JB.06465-11;
RA Mardanov A.V., Gumerov V.M., Slobodkina G.B., Beletsky A.V.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of strain 1860, a crenarchaeon of the genus
RT pyrobaculum able to grow with various electron acceptors.";
RL J. Bacteriol. 194:727-728(2012).
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; CP003098; AET32754.1; -; Genomic_DNA.
DR AlphaFoldDB; G7VDG9; -.
DR STRING; 1104324.P186_1325; -.
DR KEGG; pyr:P186_1325; -.
DR eggNOG; arCOG00252; Archaea.
DR HOGENOM; CLU_023810_3_2_2; -.
DR BioCyc; PSP1104324:GJSN-1299-MONOMER; -.
DR Proteomes; UP000005867; 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:SF5; 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 345..448
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 461 AA; 49403 MW; 5D285E8EAD9B663F CRC64;
MVTFLKKVIS TPVLADLLRR GELVVAVYGL GYVGMALSAA WALAGARVIG VDINSGKVEK
LNSGVVEYVE KDVVDVLTHA IRSGKFTATT DGVVASIRSH VKIVAVPVFL KKSATAIDVD
FSALTSAAKS IGAGLKKGDL VIVESSVPPG TTEEVVRSVL EGASGLVAEE DFYLAYSPER
VMVGHALKDI VENYPKVVAG VGPRSAEEAA ELYRQVAKRG VLVLESTREA EFEKLLEGVY
RDVNIAVANE MAKLANTLGI SFRRAREAAN SQPYSHVHKP GSGVGGNCIP VYPYFLMWTA
AKYGVDLPLT RTARFINEKQ PEEVAFAALR AMLKHGVNPA AAKIVILGLA FRGDVDDTRG
SPTYDIIATL LKVGIKSEQI TVHDPYVKQD MLLARWGIAL TQDLESAVKG ADVVIISTDH
SAYKIKASVL LSLMNSQVVV DARGVLTPDA DIYSIDSGRW P
//
