ID   A4TDY1_MYCGI            Unreviewed;       410 AA.
AC   A4TDY1;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=(1->4)-alpha-D-glucan synthase (ADP-glucose) {ECO:0000313|EMBL:ABP46731.1};
GN   OrderedLocusNames=Mflv_4262 {ECO:0000313|EMBL:ABP46731.1};
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP46731.1};
RN   [1] {ECO:0000313|EMBL:ABP46731.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP46731.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABP46731.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP46731.1};
RX   PubMed=23469141;
RA   Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT   "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT   Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT   during Pyrene Degradation.";
RL   PLoS ONE 8:E58066-E58066(2013).
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DR   EMBL; CP000656; ABP46731.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4TDY1; -.
DR   STRING; 350054.Mflv_4262; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   KEGG; mgi:Mflv_4262; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_2_3_11; -.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   CDD; cd03801; GT4_PimA-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR028098; Glyco_trans_4-like_N.
DR   PANTHER; PTHR45947; SULFOQUINOVOSYL TRANSFERASE SQD2; 1.
DR   PANTHER; PTHR45947:SF3; SULFOQUINOVOSYL TRANSFERASE SQD2; 1.
DR   Pfam; PF13439; Glyco_transf_4; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          17..199
FT                   /note="Glycosyltransferase subfamily 4-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13439"
FT   DOMAIN          210..366
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   REGION          391..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..410
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   410 AA;  44176 MW;  85D7143A75CA2269 CRC64;
     MKMKILLVSW EYPPVVIGGL GRHVHHLATE LVAAGHEVVV LSRRPTGTDP QTHPTTDETH
     EGVRVIAAAE DPHEFGFGTD MMAWVLAMGH SMIRAGFGLD GWRPDIVHAH DWLVAHPAVA
     LAQFFDVPLV STIHATEAGR HSGWVSGSVS RQVHALESWL VRDSDSLITC SASMRDEISA
     LFGPELAEIS VIPNGIDTDG WPFAARRAHS GPAELLYFGR LEYEKGVHDA IAALPKVRRT
     HPGTTLTIAG DGTQLGFLTE QARRHKVLKA TKFVGRVDHS QLLTLLHRAD VAVLPSHYEP
     FGIVALEAAA TGTPLVTSTA GGLGEAVIDG VTGMSYPPSD VIALAAAIRA VLDAPAAAQE
     RATAARARLT SDFAWHTVAA ETAQVYLAAK RAERRPQPRR TIVERPLPDR
//