ID   AGLF_HALVD              Reviewed;         243 AA.
AC   D4GYH1; B2G4W5;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=UTP--glucose-1-phosphate uridylyltransferase AglF;
DE            EC=2.7.7.9;
DE   AltName: Full=Archaeal glycosylation protein F;
GN   Name=aglF; OrderedLocusNames=HVO_1527;
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 IN GLYCOSYLATION, AND GENE
RP   NAME.
RC   STRAIN=DS2 / DS70;
RX   PubMed=18631242; DOI=10.1111/j.1365-2958.2008.06352.x;
RA   Yurist-Doutsch S., Abu-Qarn M., Battaglia F., Morris H.R., Hitchen P.G.,
RA   Dell A., Eichler J.;
RT   "AglF, aglG and aglI, novel members of a gene island involved in the N-
RT   glycosylation of the Haloferax volcanii S-layer glycoprotein.";
RL   Mol. Microbiol. 69:1234-1245(2008).
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, CATALYTIC ACTIVITY, AND PATHWAY.
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   [4]
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 acid found at position 3 of the
CC       pentasaccharide. {ECO:0000269|PubMed:18631242,
CC       ECO:0000269|PubMed:20487296, ECO:0000269|PubMed:22730124}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-
CC         alpha-D-glucose; Xref=Rhea:RHEA:19889, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:58601,
CC         ChEBI:CHEBI:58885; EC=2.7.7.9;
CC         Evidence={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 UDPGP type 2 family. {ECO:0000305}.
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DR   EMBL; AM991128; CAQ51229.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE04323.1; -; Genomic_DNA.
DR   RefSeq; WP_004041405.1; NC_013967.1.
DR   AlphaFoldDB; D4GYH1; -.
DR   SMR; D4GYH1; -.
DR   STRING; 309800.C498_02990; -.
DR   EnsemblBacteria; ADE04323; ADE04323; HVO_1527.
DR   GeneID; 8924609; -.
DR   KEGG; hvo:HVO_1527; -.
DR   eggNOG; arCOG00664; Archaea.
DR   HOGENOM; CLU_029499_2_0_2; -.
DR   OMA; MHYVRQG; -.
DR   OrthoDB; 78828at2157; -.
DR   BioCyc; MetaCyc:MON-19292; -.
DR   UniPathway; UPA00977; -.
DR   Proteomes; UP000008243; Chromosome.
DR   GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0045232; P:S-layer organization; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..243
FT                   /note="UTP--glucose-1-phosphate uridylyltransferase AglF"
FT                   /id="PRO_0000415423"
SQ   SEQUENCE   243 AA;  27535 MW;  6AA3AC63E053AA35 CRC64;
     MQAVVLAAGK GTRLRPLTED KPKGMVEVDG KPILTHCFDQ LVDLGAEKLV VVVGYKKEII
     IQHYDDEYRG VPITYAHQRE QKGLAHALLT VEDHIDEDFM LMLGDNIFNA NLGDVVKRQR
     EDRADAAFLV EEVDWDEASR YGVCVTNDYG EITEVIEKPE EPPSNLVMTG FYTFTPAIFH
     ACHLVQPSNR GEYEISEAID LLIRSGRTID AIRIDGWRLD IGYPEDRDEA EQRLQEETTQ
     ATE