ID   AGLM_HALVD              Reviewed;         430 AA.
AC   D4GYH5; C3W971;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=UDP-glucose 6-dehydrogenase AglM;
DE            Short=UDP-Glc dehydrogenase;
DE            Short=UDP-GlcDH;
DE            Short=UDPGDH;
DE            EC=1.1.1.22;
DE   AltName: Full=Archaeal glycosylation protein M;
GN   Name=aglM; OrderedLocusNames=HVO_1531;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, PATHWAY, AND GENE NAME.
RC   STRAIN=DS2 / DS70;
RX   PubMed=20487296; DOI=10.1111/j.1365-2958.2009.07045.x;
RA   Yurist-Doutsch S., Magidovich H., Ventura V.V., Hitchen P.G., Dell A.,
RA   Eichler J.;
RT   "N-glycosylation in Archaea: on the coordinated actions of Haloferax
RT   volcanii AglF and AglM.";
RL   Mol. Microbiol. 75:1047-1058(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC   VKM B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [3]
RP   FUNCTION IN GLYCOSYLATION OF FLAGELLINS, AND DISRUPTION PHENOTYPE.
RC   STRAIN=H53;
RX   PubMed=22730124; DOI=10.1128/jb.00731-12;
RA   Tripepi M., You J., Temel S., Onder O., Brisson D., Pohlschroder M.;
RT   "N-glycosylation of Haloferax volcanii flagellins requires known Agl
RT   proteins and is essential for biosynthesis of stable flagella.";
RL   J. Bacteriol. 194:4876-4887(2012).
CC   -!- FUNCTION: Involved in the assembly of a N-linked pentasaccharide that
CC       decorates the S-layer glycoprotein and flagellins. Involved in the
CC       biosynthesis of the hexuronic acids found at both positions 2 and 3 of
CC       the pentasaccharide. {ECO:0000269|PubMed:20487296,
CC       ECO:0000269|PubMed:22730124}.
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:0000269|PubMed:20487296};
CC   -!- ACTIVITY REGULATION: Activity improves as salinity decreases.
CC       {ECO:0000269|PubMed:20487296}.
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:0000269|PubMed:20487296}.
CC   -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC       {ECO:0000269|PubMed:20487296}.
CC   -!- DISRUPTION PHENOTYPE: Mutants exhibit defective or limited motility.
CC       {ECO:0000269|PubMed:22730124}.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; FN386609; CAY46591.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE05103.1; -; Genomic_DNA.
DR   RefSeq; WP_004041409.1; NZ_AOHU01000028.1.
DR   AlphaFoldDB; D4GYH5; -.
DR   SMR; D4GYH5; -.
DR   STRING; 309800.HVO_1531; -.
DR   PaxDb; 309800-C498_03010; -.
DR   EnsemblBacteria; ADE05103; ADE05103; HVO_1531.
DR   GeneID; 8924832; -.
DR   KEGG; hvo:HVO_1531; -.
DR   eggNOG; arCOG00253; Archaea.
DR   HOGENOM; CLU_023810_1_1_2; -.
DR   OrthoDB; 59839at2157; -.
DR   BioCyc; MetaCyc:MONOMER-19291; -.
DR   BRENDA; 1.1.1.22; 2561.
DR   UniPathway; UPA00038; UER00491.
DR   UniPathway; UPA00977; -.
DR   Proteomes; UP000008243; 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:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
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   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..430
FT                   /note="UDP-glucose 6-dehydrogenase AglM"
FT                   /id="PRO_0000415417"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   430 AA;  45967 MW;  BC8ABB67E71DFF7F CRC64;
     MELSIIGSGY VGTTIAACFA ELGHDVVNVD IDEDIVASLN DGQAPIHEPG LAELVERYAG
     DRLRATTDYD EILDTDATFL ALPTPSTDDG SIDLGAMKTA ATSLGETLAR KDDSHLVVTK
     STVVPRTTVD VIGPRIEEAS GKRVGDGLDI AMNPEFLREG TAVDDFLSPD KIVLGAQTDR
     AYETLAEIFA PLVERAGNPP VVKTGISEAE MIKYANNAFL ASKISLANDL ANICKVFGVD
     SAEVLESIGL DSRIGSAFLG AGLGWGGSCF PKDTAAIIAA ARAQGYEPRL LQAAVDVNDG
     QPERMLDLLR ERFDLDGKRV AVLGLAFKPG TDDIRKSRAI LLIQALLDAG ADVVGYDPVA
     TENMRERFPD IDYADSAADA LANADAALVA TDWDEFAALD DEFDAMRERI VIDGRRIVTR
     REGLDYESLV
//