ID Q2S192_SALRD Unreviewed; 427 AA.
AC Q2S192;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=ADP-glucose pyrophosphorylase {ECO:0000313|EMBL:ABC44137.1};
GN OrderedLocusNames=SRU_1929 {ECO:0000313|EMBL:ABC44137.1};
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC44137.1, ECO:0000313|Proteomes:UP000008674};
RN [1] {ECO:0000313|EMBL:ABC44137.1, ECO:0000313|Proteomes:UP000008674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31
RC {ECO:0000313|Proteomes:UP000008674};
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443}.
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DR EMBL; CP000159; ABC44137.1; -; Genomic_DNA.
DR RefSeq; WP_011404664.1; NC_007677.1.
DR RefSeq; YP_446039.1; NC_007677.1.
DR AlphaFoldDB; Q2S192; -.
DR STRING; 309807.SRU_1929; -.
DR EnsemblBacteria; ABC44137; ABC44137; SRU_1929.
DR KEGG; sru:SRU_1929; -.
DR PATRIC; fig|309807.25.peg.1998; -.
DR eggNOG; COG0448; Bacteria.
DR HOGENOM; CLU_029499_14_4_10; -.
DR OrthoDB; 9801810at2; -.
DR Proteomes; UP000008674; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-EC.
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; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR NCBIfam; TIGR02091; glgC; 1.
DR PANTHER; PTHR43523:SF12; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE LARGE SUBUNIT 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43523; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE-RELATED; 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; PS00808; ADP_GLC_PYROPHOSPH_1; 1.
DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
DR PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008674};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..273
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 427 AA; 47777 MW; 1FC64172DBB5CD43 CRC64;
MSTSLDNSIL TVILGGGKGT RLYPLTKLRA KPAVPLAGRY RLIDVPVSTS INSGITRIFV
LTQYNSASLN RHLARAYQFD RFSNGFVSIL AAEQTPSSKD WFQGTADAVR RSLPHIEGHR
HRHVLILSGD QLYSMDYRKM LAHHRETDAD VTLGTIPVAA DDATSFGILK TDDEHIITEF
HEKPDRDELD GLESPVGPGL EDEGRVYHAS MGMYIFDREP LHELLNANPN DHDFGNQIIP
KAIDKMRVAS YPFSDYWSDI GTIRSFYEAN LMLAEPEPPF SLYDPNRPLY TRARMLPPAK
VQNSTVQDSL ITEGSLVENS QISKSVVGIR SYVGPDTTLK NTVMMGADHF RWHDMEERGF
VEGPANPGIG ENSYVEGAII DKNVSIGKRC IIKNRDNVQE AEEDLYHIRD GIVVIPKNTR
IPDDTII
//
