AGLM_HALVD
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 03-AUG-2022, entry version 63.
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 / VKM
RC 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}.
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; FN386609; CAY46591.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE05103.1; -; Genomic_DNA.
DR RefSeq; WP_004041409.1; NC_013967.1.
DR AlphaFoldDB; D4GYH5; -.
DR SMR; D4GYH5; -.
DR STRING; 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 OMA; CECLNLP; -.
DR OrthoDB; 47911at2157; -.
DR BioCyc; MetaCyc:MON-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 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 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; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52413; SSF52413; 1.
DR TIGRFAMs; TIGR03026; NDP-sugDHase; 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
