AGL12_HALVD
ID AGL12_HALVD Reviewed; 310 AA.
AC D4GU72;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Low-salt glycan biosynthesis protein Agl12;
DE EC=4.2.1.-;
GN Name=agl12; OrderedLocusNames=HVO_2059; ORFNames=C498_05583;
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 [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 [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=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=24194539; DOI=10.1128/mbio.00716-13;
RA Kaminski L., Guan Z., Yurist-Doutsch S., Eichler J.;
RT "Two distinct N-glycosylation pathways process the Haloferax volcanii S-
RT layer glycoprotein upon changes in environmental salinity.";
RL MBio 4:E00716-E00716(2013).
CC -!- FUNCTION: Lyase involved in N-glycan biosynthetic pathway that takes
CC place under low-salt conditions (1.75 M instead of 3.4 M). Participates
CC in the formation of the tetrasaccharide present at 'Asn-532' of S-layer
CC glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and
CC rhamnose. Involved in the addition of final rhamnose (sugar 4) of the
CC tetrasaccharide on the dolichol phosphate carrier.
CC {ECO:0000269|PubMed:24194539}.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:24194539}.
CC -!- PATHWAY: Cell surface structure biogenesis; S-layer biogenesis.
CC {ECO:0000269|PubMed:24194539}.
CC -!- DISRUPTION PHENOTYPE: Impaired formation of the tetrasaccharide present
CC at 'Asn-532' of S-layer glycoprotein Csg. No effect on 'Asn-47' and
CC 'Asn-117' glycosylation of S-layer glycoprotein Csg.
CC {ECO:0000269|PubMed:24194539}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. dTDP-glucose dehydratase subfamily. {ECO:0000305}.
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DR EMBL; CP001956; ADE03524.1; -; Genomic_DNA.
DR EMBL; AOHU01000040; ELY33653.1; -; Genomic_DNA.
DR RefSeq; WP_004041944.1; NZ_AOHU01000040.1.
DR AlphaFoldDB; D4GU72; -.
DR SMR; D4GU72; -.
DR STRING; 309800.C498_05583; -.
DR EnsemblBacteria; ADE03524; ADE03524; HVO_2059.
DR EnsemblBacteria; ELY33653; ELY33653; C498_05583.
DR GeneID; 8924604; -.
DR KEGG; hvo:HVO_2059; -.
DR PATRIC; fig|309800.29.peg.1083; -.
DR eggNOG; arCOG01371; Archaea.
DR HOGENOM; CLU_007383_1_14_2; -.
DR OMA; KLIPLMC; -.
DR OrthoDB; 43299at2157; -.
DR BioCyc; MetaCyc:MON-18752; -.
DR UniPathway; UPA00378; -.
DR UniPathway; UPA00977; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:InterPro.
DR GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
DR CDD; cd05246; dTDP_GD_SDR_e; 1.
DR InterPro; IPR005888; dTDP_Gluc_deHydtase.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01181; dTDP_gluc_dehyt; 1.
PE 3: Inferred from homology;
KW Lyase; NAD; Reference proteome.
FT CHAIN 1..310
FT /note="Low-salt glycan biosynthesis protein Agl12"
FT /id="PRO_0000428775"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 124
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 7..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 32..35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 58..59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 122..124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 146..150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 185..186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201..203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 269..272
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 310 AA; 34141 MW; E1F98163E469D63D CRC64;
MDVLVTGGAG FIGSNFVRYL LDNSDDSVVT LDALTYAGSR DNLAGYLDHP NHRFVEGDIR
DRELVDDLVA DADVIVNFAA ESHVDRSIGG AEPFVSTNVQ GTQTLLDAAL DADIDRFLQI
STDEVYGEIH DGKFTEDDPL APRNPYSATK AGADLLVRSY RETHDLPTLI TRTCNNFGPR
QHPEKLIPKF IQRAANGETL PVYGDGSNVR EWIYVEDNCA ALDVVLREGD IGEVYNIGSG
VELSNLETTE KILEAVGGSE DQIEFVEDRA GHDQRYAIDA TKTKALGWEP EWSFEDGLEA
CVDYYLGDDE
