ID F8KY84_PARAV Unreviewed; 437 AA.
AC F8KY84;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000313|EMBL:CCB85819.1};
DE EC=2.7.7.27 {ECO:0000313|EMBL:CCB85819.1};
GN Name=glgC {ECO:0000313|EMBL:CCB85819.1};
GN OrderedLocusNames=PUV_08690 {ECO:0000313|EMBL:CCB85819.1};
OS Parachlamydia acanthamoebae (strain UV7).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Parachlamydia.
OX NCBI_TaxID=765952 {ECO:0000313|EMBL:CCB85819.1, ECO:0000313|Proteomes:UP000000495};
RN [1] {ECO:0000313|EMBL:CCB85819.1, ECO:0000313|Proteomes:UP000000495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UV7 {ECO:0000313|Proteomes:UP000000495};
RX PubMed=21690563; DOI=10.1093/molbev/msr161;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S., Horn M.;
RT "Unity in variety--the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 28:3253-3270(2011).
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443}.
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DR EMBL; FR872580; CCB85819.1; -; Genomic_DNA.
DR RefSeq; WP_013924610.1; NC_015702.1.
DR AlphaFoldDB; F8KY84; -.
DR STRING; 765952.PUV_08690; -.
DR KEGG; puv:PUV_08690; -.
DR eggNOG; COG0448; Bacteria.
DR HOGENOM; CLU_029499_14_4_0; -.
DR Proteomes; UP000000495; 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; 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};
KW Nucleotidyltransferase {ECO:0000313|EMBL:CCB85819.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000495};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCB85819.1}.
FT DOMAIN 30..289
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT UNSURE 191
FT /note="D or N"
FT /evidence="ECO:0000313|EMBL:CCB85819.1"
SQ SEQUENCE 437 AA; 49205 MW; 1CBFA5250E6B2A69 CRC64;
MSLLTTPHVK TTPLTQTINL HTHRTDRVAS IILGGGEGVR LFPLTLSRCK PAIPVGGRYR
LIDFSISNSL NSGYQKIFIL TQFLSSSLHQ HIFRTYQFDP FSGGFIELLP AEQKPHKKTW
YQGTADAVRQ SLECFIETPV DYFLILSGDQ LYNMDFRPML QFAHENDADL VVASHPVNAK
DASRMGILKV DQDFQIKDFC EKPKTQEELD PFYLPNAEGK NYLGSMGIYL FKREVLFDLL
LTDSREDFGK HLIPTKVKEG GVYTYIHHGY WEDIGTIGSF YEANIALTQV NPHFNCYDET
YPIYTSRSYL PGAKISNSQI NQSIICEGSI VEASSISNTI LGPRSVIKKG AIIRDSYVMG
NEFYTPPVQI KNRPSTLSIG KDCVIEHAII DKYVNIGDGV QLINKDRLTT YDGEHVFIRD
GVIIVPRGAD LPDGFII
//
