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Database: UniProt
Entry: A0A1H9GWW6_9EURY
LinkDB: A0A1H9GWW6_9EURY
Original site: A0A1H9GWW6_9EURY 
ID   A0A1H9GWW6_9EURY        Unreviewed;       466 AA.
AC   A0A1H9GWW6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=SAMN04489841_2020 {ECO:0000313|EMBL:SEQ54524.1};
OS   Natrinema salaciae.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=1186196 {ECO:0000313|EMBL:SEQ54524.1, ECO:0000313|Proteomes:UP000199114};
RN   [1] {ECO:0000313|Proteomes:UP000199114}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25055 {ECO:0000313|Proteomes:UP000199114};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOFD01000002; SEQ54524.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9GWW6; -.
DR   STRING; 1186196.SAMN04489841_2020; -.
DR   OrthoDB; 372050at2157; -.
DR   Proteomes; UP000199114; 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-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   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          353..453
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   466 AA;  50097 MW;  B4F0AB988D96DBE9 CRC64;
     MTTIISDTEN RADERESDQH PRDASGNGTA LEHTDARSTR SATICVVGLG YVGLPLAVGF
     AQSNYRVIGY DVDDVTVGRL QEGIDTTGDL SDEAVRDDDI SYTTDATEIG GADYVVIAVP
     TPIDDDDRPD LGYIESAATT VGSKMDPGTT VVLESTVYPG ATREVLVPAL EDASGLTAGE
     DFFVGYSPER ATPGDENHGL EDVVKVVSAQ NEKVLEDVAT LYESIVDAGV HRAPSIEVAE
     ACKVIENIQR DVNIALVNEL SMAFERLGID TREVLDAAGT KWNFHDYRPG LVGGHCIPID
     PYFFAHRATR AGADPELIRT SRAVNESMPN HVAELTIKAL NQCHKTLRES RVLVLGLAYK
     ADVGDIRSSK VADVVDHLRE FGIDVAGYDP HAEADAVRNA FDIDVQDSLT FDGFDAVLLT
     TGHSAFEEFD LDDVAAALDD DAALVDVVGA FESDDADDAD LVYRSL
//
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