ID   NGT_ACTP7               Reviewed;         620 AA.
AC   B3H2N2;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=UDP-glucose:protein N-beta-glucosyltransferase;
DE            Short=UDP-Glc:protein N-glucosyltransferase;
DE            EC=2.4.1.-;
DE   AltName: Full=HMW1C-like protein;
DE   AltName: Full=N-glycosyltransferase;
DE            Short=NGT;
GN   OrderedLocusNames=APP7_1697;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, PATHWAY, COFACTOR, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=AP76;
RX   PubMed=21852240; DOI=10.1074/jbc.m111.277160;
RA   Schwarz F., Fan Y.Y., Schubert M., Aebi M.;
RT   "Cytoplasmic N-glycosyltransferase of Actinobacillus pleuropneumoniae is an
RT   inverting enzyme and recognizes the NX(S/T) consensus sequence.";
RL   J. Biol. Chem. 286:35267-35274(2011).
CC   -!- FUNCTION: Inverting glycosyltransferase that catalyzes the transfer of
CC       one glucose moiety from UDP-glucose to an asparagine residue in
CC       peptides and proteins containing the NX(S/T) motif, resulting in their
CC       modification with a beta-linked 1,N-glucose. Likely acts as a key
CC       component of a general protein glycosylation system. Also accepts UDP-
CC       galactose as a substrate donor, albeit with low efficiency. Cannot use
CC       UDP-GlcNAc or UDP-GalNAc as substrate donor.
CC       {ECO:0000269|PubMed:21852240}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-asparaginyl-[protein] + UDP-alpha-D-glucose = H(+) + N(4)-
CC         (beta-D-glucosyl)-L-asparaginyl-[protein] + UDP;
CC         Xref=Rhea:RHEA:45952, Rhea:RHEA-COMP:11400, Rhea:RHEA-COMP:12804,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:50347, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885, ChEBI:CHEBI:85501;
CC         Evidence={ECO:0000269|PubMed:21852240};
CC   -!- COFACTOR:
CC       Note=Does not require a metal cofactor. {ECO:0000269|PubMed:21852240};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:21852240}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:21852240}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 41 family.
CC       {ECO:0000305}.
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DR   EMBL; CP001091; ACE62349.1; -; Genomic_DNA.
DR   RefSeq; WP_012478567.1; NC_010939.1.
DR   AlphaFoldDB; B3H2N2; -.
DR   SMR; B3H2N2; -.
DR   CAZy; GT41; Glycosyltransferase Family 41.
DR   EnsemblBacteria; ACE62349; ACE62349; APP7_1697.
DR   KEGG; apa:APP7_1697; -.
DR   HOGENOM; CLU_441347_0_0_6; -.
DR   OMA; MKLNPYF; -.
DR   BioCyc; APLE537457:APP7_RS08800-MON; -.
DR   UniPathway; UPA00378; -.
DR   PHI-base; PHI:6867; -.
DR   Proteomes; UP000001226; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
DR   InterPro; IPR040542; HMW1_D2.
DR   InterPro; IPR041109; HMW1C_N.
DR   Pfam; PF18254; HMw1_D2; 1.
DR   Pfam; PF18071; HMW1C_N; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycosyltransferase; Transferase.
FT   CHAIN           1..620
FT                   /note="UDP-glucose:protein N-beta-glucosyltransferase"
FT                   /id="PRO_0000430337"
SQ   SEQUENCE   620 AA;  70546 MW;  B06CE1C932368023 CRC64;
     MENENKPNVA NFEAAVAVKD YEKACSELLL ILSQLDSNFG GIQEIEFEYP VQLQDLEQEK
     IVYFCTRMAT AITTLFSDPV LEISDLGVQR FLVYQRWLAL IFASSPFVNA DHILQTYNRE
     PNRKNSLEIH LDSSKSSLIK FCILYLPESN VNLNLDVMWN ISPELCASLC FALQSPRFIG
     TSTAFNKRAT ILQWFPRHLD QLKNLNNIPS AISHDVYMHC SYDTSVNKHD VKRALNHVIR
     RHIESEYGWK DRYVAHIGYR NNKPVMVVLL EHFHSAHSIY RTHSTSMIAA REHFYLIGLG
     SPSVDQAGQE VFDEFHLVAG DNMKQKLEFI RSVCESNGAA IFYMPSIGMD MTTIFASNTR
     LAPIQAIALG HPATTHSDFI EYVIVEDDYV GSEACFSETL LRLPKDALPY VPSALAPEKV
     DYLLRENPEV VNIGIASTTM KLNPYFLEAL KAIRDRAKVK VHFHFALGQS NGITHPYVER
     FIKSYLGDSA TAHPHSPYHQ YLRILHNCDM MVNPFPFGNT NGIIDMVTLG LVGVCKTGAE
     VHEHIDEGLF KRLGLPEWLI ANTVDEYVER AVRLAENHQE RLELRRYIIE NNGLNTLFTG
     DPRPMGQVFL EKLNAFLKEN