ID B7AUR8_9FIRM Unreviewed; 373 AA.
AC B7AUR8;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=Nucleotidyl transferase domain-containing protein {ECO:0000259|Pfam:PF00483};
GN ORFNames=BACPEC_02466 {ECO:0000313|EMBL:EEC55959.1};
OS [Bacteroides] pectinophilus ATCC 43243.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=483218 {ECO:0000313|EMBL:EEC55959.1, ECO:0000313|Proteomes:UP000003136};
RN [1] {ECO:0000313|EMBL:EEC55959.1, ECO:0000313|Proteomes:UP000003136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43243 {ECO:0000313|EMBL:EEC55959.1,
RC ECO:0000313|Proteomes:UP000003136};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides pectinophilus (ATCC 43243).";
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEC55959.1, ECO:0000313|Proteomes:UP000003136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43243 {ECO:0000313|EMBL:EEC55959.1,
RC ECO:0000313|Proteomes:UP000003136};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABVQ01000037; EEC55959.1; -; Genomic_DNA.
DR AlphaFoldDB; B7AUR8; -.
DR STRING; 483218.BACPEC_02466; -.
DR eggNOG; COG0448; Bacteria.
DR HOGENOM; CLU_029499_14_0_9; -.
DR Proteomes; UP000003136; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:InterPro.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR CDD; cd02508; ADP_Glucose_PP; 1.
DR CDD; cd04651; LbH_G1P_AT_C; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR011831; ADP-Glc_PPase.
DR InterPro; IPR005836; ADP_Glu_pyroP_CS.
DR InterPro; IPR011832; GlgDAde_trans.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR NCBIfam; TIGR02092; glgD; 1.
DR PANTHER; PTHR43523; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR43523:SF6; GLYCOGEN BIOSYNTHESIS PROTEIN GLGD; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 5..255
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 373 AA; 42427 MW; B6E1D4DD879B80AC CRC64;
MRAIGIILAG GNNKMMKELS NKRAIAAMPI AGSYRSIDFA LSNMSNSHIS KVAVITQYNA
RSLNEHLSSS KWWDFGRKQG GLFVFTPTIT ADSSYWYRGT ADSLYQNLHF LKTSHEPYVV
IASGDGVYKL DYGKVLEYHI EKKADITMVV KKLDDKEDLK RFGLVSMSPE GRITEIDEKP
IETNLTTASI GVYVIRRRLL IELIEKAAEE DRHDFVKDIL IRYKNLKRIY GYKLDTYWSN
ISTVNSYYKT NMDFLDKDIR NYFFKEYPDI YSKVDDLPPA KYNYGANVKN SLVASGCIIN
GMVENSVLFK KVYIGNNSVI KNSIILNNTY IGDNAYIENC IVESNGTIKA NTRHVGEESE
PKIVIENGIS YFS
//