AGL3_SULAC
ID AGL3_SULAC Reviewed; 393 AA.
AC Q4JBJ3;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=UDP-sulfoquinovose synthase {ECO:0000303|PubMed:22059775};
DE EC=3.13.1.1 {ECO:0000269|PubMed:22059775, ECO:0000269|PubMed:25605538};
GN Name=agl3 {ECO:0000303|PubMed:22059775};
GN OrderedLocusNames=Saci_0423 {ECO:0000312|EMBL:AAY79836.1};
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=MW001;
RX PubMed=22059775; DOI=10.1111/j.1365-2958.2011.07875.x;
RA Meyer B.H., Zolghadr B., Peyfoon E., Pabst M., Panico M., Morris H.R.,
RA Haslam S.M., Messner P., Schaeffer C., Dell A., Albers S.V.;
RT "Sulfoquinovose synthase - an important enzyme in the N-glycosylation
RT pathway of Sulfolobus acidocaldarius.";
RL Mol. Microbiol. 82:1150-1163(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF HIS-95; ARG-100;
RP THR-144; MET-145; GLU-147; TYR-148; SER-180; TYR-182; THR-185 AND LYS-186.
RX PubMed=25605538; DOI=10.1007/s00792-015-0730-9;
RA Zolghadr B., Gasselhuber B., Windwarder M., Pabst M., Kracher D.,
RA Kerndl M., Zayni S., Hofinger-Horvath A., Ludwig R., Haltrich D.,
RA Oostenbrink C., Obinger C., Kosma P., Messner P., Schaeffer C.;
RT "UDP-sulfoquinovose formation by Sulfolobus acidocaldarius.";
RL Extremophiles 19:451-467(2015).
CC -!- FUNCTION: Catalyzes the biosynthesis of UDP-sulfoquinovose by the
CC transfer of sulfite to UDP-glucose (PubMed:22059775, PubMed:25605538).
CC Important for the assembly of the S-layer N-glycans (PubMed:22059775).
CC The reaction probably occurs through an NAD(+)-dependent
CC oxidation/dehydration/enolization/sulfite addition process
CC (PubMed:25605538). In vitro, in the absence of sulfite, UDP-D-glucose
CC is converted via UDP-4-keto-D-glucose to UDP-D-glucose-5,6-ene
CC (PubMed:25605538). {ECO:0000269|PubMed:22059775,
CC ECO:0000269|PubMed:25605538}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + sulfite + UDP-alpha-D-glucose = H2O + UDP-alpha-D-6-
CC sulfoquinovose; Xref=Rhea:RHEA:13197, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:60009; EC=3.13.1.1;
CC Evidence={ECO:0000269|PubMed:22059775, ECO:0000269|PubMed:25605538};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:25605538};
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene results in a significant
CC change in the size of the S-layer SlaA and the flagellin FlaB
CC glycoproteins. Mutant has a significantly lower growth rate at elevated
CC salt concentrations. {ECO:0000269|PubMed:22059775}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; CP000077; AAY79836.1; -; Genomic_DNA.
DR RefSeq; WP_011277338.1; NC_007181.1.
DR AlphaFoldDB; Q4JBJ3; -.
DR SMR; Q4JBJ3; -.
DR STRING; 330779.Saci_0423; -.
DR EnsemblBacteria; AAY79836; AAY79836; Saci_0423.
DR GeneID; 3473183; -.
DR KEGG; sai:Saci_0423; -.
DR PATRIC; fig|330779.12.peg.421; -.
DR eggNOG; arCOG04762; Archaea.
DR HOGENOM; CLU_040971_1_0_2; -.
DR OMA; IHFAEQR; -.
DR BRENDA; 3.13.1.1; 6160.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0046507; F:UDPsulfoquinovose synthase activity; IEA:UniProtKB-EC.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Hydrolase; NAD; Reference proteome.
FT CHAIN 1..393
FT /note="UDP-sulfoquinovose synthase"
FT /id="PRO_0000444048"
FT ACT_SITE 144
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT ACT_SITE 186
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 31..35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 74..75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 212
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 238..241
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 253..255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT BINDING 326..328
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O48917"
FT MUTAGEN 95
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25605538"
FT MUTAGEN 100
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25605538"
FT MUTAGEN 144
FT /note="T->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:25605538"
FT MUTAGEN 145
FT /note="M->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25605538"
FT MUTAGEN 147
FT /note="E->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:25605538"
FT MUTAGEN 148
FT /note="Y->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:25605538"
FT MUTAGEN 180
FT /note="S->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:25605538"
FT MUTAGEN 182
FT /note="Y->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25605538"
FT MUTAGEN 185
FT /note="T->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:25605538"
FT MUTAGEN 186
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25605538"
SQ SEQUENCE 393 AA; 45016 MW; EBA14B47049105F0 CRC64;
MRILVLGIDG HLGWPLALRL AKRGHEVIGI DNLSTRRFSE EVGSDSAFPL PQPQERVSEA
KKHLGVDITF YVGDITNYGF FKDIVQRYKP DAIVHFAEQR SAPYSMIDMD HAVYTVINNE
VSTLRVIQAV LEVDPTIHIL KMGTMGEYGT PAFDIPESIY VEAIVNGKKD KIIVPRKAGS
VYHWTKVHDT DFLLHFQELY GLTVTDIMQG PVYGTRTEEI VEETLRTRFD FDEVWGTVVN
RYCVEAILGL PLTVYGKGGQ TRGFISLEDS IQALTLLLEN PPKQGEYRVA NQFAEIYSVK
KIAEFVKKAG EELGLNVEIG SYENPRVEAE EHYYNPERKV LPSLGFYPKK RLPEDVKIMI
KDLLPYKTRL ERFKHVILPK TKWRKPQYVK RVR
