ID   OGT1_GIAIC              Reviewed;        1480 AA.
AC   A8BFN4;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase;
DE            Short=GlOGT {ECO:0000303|PubMed:18948359};
DE            EC=2.4.1.255 {ECO:0000269|PubMed:18948359};
DE   AltName: Full=O-linked GlcNAc transferase {ECO:0000312|EMBL:EDO79630.1};
DE   AltName: Full=O-linked N-acetylglucosaminyltransferase {ECO:0000303|PubMed:18948359};
GN   ORFNames=GL50803_12081;
OS   Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=184922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50803 / WB clone C6;
RX   PubMed=17901334; DOI=10.1126/science.1143837;
RA   Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D.,
RA   Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J.,
RA   Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U.,
RA   Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E.J., Palm D.,
RA   Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J.,
RA   Svard S.G., Sogin M.L.;
RT   "Genomic minimalism in the early diverging intestinal parasite Giardia
RT   lamblia.";
RL   Science 317:1921-1926(2007).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 50803 / WB clone C6 {ECO:0000269|PubMed:18948359};
RX   PubMed=18948359; DOI=10.1093/glycob/cwn107;
RA   Banerjee S., Robbins P.W., Samuelson J.;
RT   "Molecular characterization of nucleocytosolic O-GlcNAc transferases of
RT   Giardia lamblia and Cryptosporidium parvum.";
RL   Glycobiology 19:331-336(2009).
CC   -!- FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine from
CC       UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear
CC       proteins resulting in their modification with a beta-linked N-
CC       acetylglucosamine (O-GlcNAc). {ECO:0000269|PubMed:18948359}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-
CC         acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H(+) + UDP;
CC         Xref=Rhea:RHEA:48904, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:90838; EC=2.4.1.255;
CC         Evidence={ECO:0000269|PubMed:18948359};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-
CC         (N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP;
CC         Xref=Rhea:RHEA:48908, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:12252,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:90840; EC=2.4.1.255;
CC         Evidence={ECO:0000269|PubMed:18948359};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.8 uM for UDP-GlcNAc {ECO:0000269|PubMed:18948359};
CC         Vmax=5.1 pmol/min/mg enzyme {ECO:0000269|PubMed:18948359};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:18948359}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18948359}. Nucleus
CC       {ECO:0000269|PubMed:18948359}.
CC   -!- DOMAIN: The TPR repeat domain is required for substrate binding and
CC       oligomerization. {ECO:0000250|UniProtKB:O15294}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 41 family. O-GlcNAc
CC       transferase subfamily. {ECO:0000305}.
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DR   EMBL; AACB02000015; EDO79630.1; -; Genomic_DNA.
DR   RefSeq; XP_001707304.1; XM_001707252.1.
DR   AlphaFoldDB; A8BFN4; -.
DR   SMR; A8BFN4; -.
DR   STRING; 5741.EDO79630; -.
DR   CAZy; GT41; Glycosyltransferase Family 41.
DR   EnsemblProtists; EDO79630; EDO79630; GL50803_12081.
DR   GeneID; 5700203; -.
DR   KEGG; gla:GL50803_0012081; -.
DR   VEuPathDB; GiardiaDB:GL50803_12081; -.
DR   HOGENOM; CLU_249719_0_0_1; -.
DR   InParanoid; A8BFN4; -.
DR   OMA; CDDINSI; -.
DR   OrthoDB; 142546at2759; -.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; IBA:GO_Central.
DR   GO; GO:0097363; F:protein O-GlcNAc transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR   Gene3D; 1.25.40.10; -; 3.
DR   InterPro; IPR037919; OGT.
DR   InterPro; IPR029489; OGT/SEC/SPY_C.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR44366; PTHR44366; 1.
DR   Pfam; PF13844; Glyco_transf_41; 2.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF13181; TPR_8; 2.
DR   SMART; SM00028; TPR; 8.
DR   SUPFAM; SSF48452; SSF48452; 3.
DR   PROSITE; PS50005; TPR; 6.
DR   PROSITE; PS50293; TPR_REGION; 4.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycosyltransferase; Nucleus; Repeat; TPR repeat; Transferase.
FT   CHAIN           1..1480
FT                   /note="UDP-N-acetylglucosamine--peptide N-
FT                   acetylglucosaminyltransferase"
FT                   /id="PRO_0000416939"
FT   REPEAT          38..71
FT                   /note="TPR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          113..146
FT                   /note="TPR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          176..209
FT                   /note="TPR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          288..321
FT                   /note="TPR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          613..646
FT                   /note="TPR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          648..680
FT                   /note="TPR 6"
FT                   /evidence="ECO:0000255"
FT   REGION          468..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1093..1128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1095..1111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1269
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:O15294"
FT   BINDING         1272
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:O15294"
FT   BINDING         1333..1336
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:O15294"
FT   BINDING         1351..1353
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:O15294"
FT   BINDING         1357
FT                   /ligand="UDP"
FT                   /ligand_id="ChEBI:CHEBI:58223"
FT                   /evidence="ECO:0000250|UniProtKB:O15294"
SQ   SEQUENCE   1480 AA;  166363 MW;  A1D3856F0EB6886F CRC64;
     MVALMDKIAQ LFRNKQYSDL IQLIDKQLHA KNEPEALIFL YAIQGEISFK QKDWIQAFAA
     YEKAVAESKQ KGLPTQVYAQ IVQRQMIILL RLQMLDTAFG LFSENQSVSV DNVQVLAQLA
     LLYLMCERYS EAEKLLSSIV ESSTSNTITL SKQFKEDIGP FKELFGVLDT YDTFLATILN
     NLAICNSKLG NHTLAFDQFQ QALDIIKDPE KITRPPLSPI TVLFDNCVST VDEDKEKALK
     VEHHMLTINE SKENQEDDTV LSLLRDGCTL IPSSTLGTHL PLIIELHSTI CYNIGKLELT
     LGNLDRSVNH FKKSIEYQPS FARYVALGLV YRDMRNFYDA AEMLTKAVDS CVGISNLCLG
     EVVYNLGILV SEELKMPYKS LQFFDEATVL FIRGEFSAGA ILSRIMKANS LTTITTATAV
     SSDWEFIMAF LNTLYLDLCA FSKDQGFNVE AAFTGTNAIS FNLPITEPQE KESPKSDKIA
     SEKPLVESNP GRSRTPSSMN DVYMLSAENL SFSLLESSFA QKETITSRLF PTFQAETKRY
     LAILYTNLGL IYYRIGIPTY YKQARRCFEV AIWFDNDCVF AINYLSVLLL KENSKTLAIE
     GLLKCTRLFP EYYEPFYNLG NILKADEENK KALQYYSRAI ELNPRFLDGY LARGVLYAEL
     HRFETAYLDF SKCIELDPDN RHAFCNYIHM KQILGIFHND TLDMRKISKI IDDYIHEYLT
     VQNAINKGVV LPSHPLPPIM PYHCYLYRLS SSQLRFICQR YSEQNVNWVK QNIDMMSTPL
     LDLSIHQRPM PPSIGLINSV SSSSQLQLSM LPLNQSAADS MVPLAMLTPG PTLCTAIGFQ
     SIKSVIRDSQ HITHGPIFSY DRALITLARS KHSSKCPISY IDIVNLKSPL RLGVLCDDIN
     SIPIGCILES WLRNIDPKVA SLSIYSTVAS DKSALRTSLE AHCSNFIDFT NYKYQNNPFL
     CAQRINGDGI CIMISMCQHN CGLEGRILAM RPAPIQISYW THGGTTNSNY LDYILADQYC
     IPPGYAHLYS EHVITMPGCF ICPSHSMHYS NAILLEEHAD ILKVTVEEVR SLIQDSKPDI
     DVNHHSAAGE NILSLDGSDA TSSSVDSGIG SRTHSEAPIG GGDKDEGAHS SKILELELEL
     AEIAKMKGET KNGVSTNSAS EGRDELLMND RILITGDNVF FQVQPIRNGR LVGGRDRSMI
     KKMEPLLKAI YPLQRIASEA AVPASMEKSE NNSDLTSHRV CLELPLYRKN IRALYGIPAN
     CFLFCTFNQV YKFDMGTLGI IAALLRSVPN AYYALLKFPP ASQLHIEAFF RHKAPDILDR
     VIFLSMLPMK VEHIRRYLAV DVFVDTLKCN GSTIVLDALW SGVPVVGFVG EYILSRKTLS
     FLSVLECKDL ICASQGEAVL LCTRLAVDSG YYFSVRKRIL KNRSNLFNIS RWCDNFVLTM
     MLAYKNWIFG GKPTSFSTER VIANVKSQGF SWPLKSTGAQ