ID Q9HQQ9_HALSA Unreviewed; 426 AA.
AC Q9HQQ9;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124};
DE EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124};
GN Name=udg1 {ECO:0000313|EMBL:AAG19454.1};
GN Synonyms=aglM1 {ECO:0000313|EMBL:DAC78167.1}, ugd1
GN {ECO:0000313|EMBL:DAC78167.1};
GN OrderedLocusNames=VNG_1048G {ECO:0000313|EMBL:AAG19454.1};
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX NCBI_TaxID=64091 {ECO:0000313|EMBL:AAG19454.1, ECO:0000313|Proteomes:UP000000554};
RN [1] {ECO:0000313|EMBL:AAG19454.1, ECO:0000313|Proteomes:UP000000554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1
RC {ECO:0000313|Proteomes:UP000000554}, and NRC-1
RC {ECO:0000313|EMBL:AAG19454.1};
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.W., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2] {ECO:0000313|EMBL:DAC78167.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC78167.1};
RX PubMed=18313895; DOI=.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
RN [3] {ECO:0000313|EMBL:DAC78167.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC78167.1};
RX PubMed=26042526;
RA Pfeiffer F., Oesterhelt D.;
RT "A manual curation strategy to improve genome annotation: application to a
RT set of haloarchael genomes.";
RL Life 5:1427-1444(2015).
RN [4] {ECO:0000313|EMBL:DAC78167.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC78167.1};
RA Pfeiffer F., Marchfelder A., Habermann B.H., Dyall-Smith M.;
RT "The genome of the Halobacterium salinarum type strain is closely related
RT to that of the laboratory strains NRC-1 and R1.";
RL Microbiol. Resour. Announc. 0:0-0(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-
CC alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00000874,
CC ECO:0000256|PIRNR:PIRNR000124};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate
CC biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step
CC 1/1. {ECO:0000256|ARBA:ARBA00004701}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00006601, ECO:0000256|PIRNR:PIRNR000124}.
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; AE004437; AAG19454.1; -; Genomic_DNA.
DR EMBL; BK010829; DAC78167.1; -; Genomic_DNA.
DR PIR; B84261; B84261.
DR RefSeq; WP_010902749.1; NC_002607.1.
DR AlphaFoldDB; Q9HQQ9; -.
DR STRING; 64091.VNG_1048G; -.
DR PaxDb; 64091-VNG_1048G; -.
DR GeneID; 68693844; -.
DR KEGG; hal:VNG_1048G; -.
DR PATRIC; fig|64091.14.peg.801; -.
DR HOGENOM; CLU_023810_1_1_2; -.
DR OrthoDB; 59839at2157; -.
DR BRENDA; 1.1.1.22; 2552.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway.
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 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; IPR028357; UDPglc_DH_bac.
DR NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR NCBIfam; NF041297; UDPGDh_AglM; 1.
DR PANTHER; PTHR43750; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 1.
DR PANTHER; PTHR43750:SF3; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 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; PIRSF500134; UDPglc_DH_bac; 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|PIRNR:PIRNR000124};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000124};
KW Reference proteome {ECO:0000313|Proteomes:UP000000554}.
FT DOMAIN 316..415
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-1"
FT BINDING 30
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 253..257
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 330
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
SQ SEQUENCE 426 AA; 44898 MW; C493147203502760 CRC64;
MDVSIVGSGY VGTTIAACFA ELGHTVVNVD VDADVVAAIN DGDAPIHEPG LAERIDAHAG
TRLRATTDYE AVRDTDVTFL ALPTPAREDG SIDTSIMESG AASLGEALAG ADDHMVVVKS
TVVPGTTEDV VESALVSAGF DDPLLAMNPE FLRMGSAVDD FRHPDKVVFG ARRDAAYDQL
HAVFEPLLAD AGDATVVETG LREAEMIKYA NNAFLASKVS LINDLGNICK ELGVDAYEVA
DAIAEDDRIS GRFLRSGVGW GGSCFPKDVA AITAAAKDAG YEPAMLEAAV EVNDRQPERL
LSLLDGHVDV AGERVAVLGL SFKPGTDDIR GTRAVPVIDG LQDREADVVA YDPVAAEKMA
EQRPEVTYAD SAAGALADAV GAVVVTDWDE FAALDDEFDA MAERVVVDGR RVVDPQADLT
YDGLTW
//
