ID A0A127W289_SPOPS Unreviewed; 368 AA.
AC A0A127W289;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000313|EMBL:AMQ07624.1};
GN ORFNames=AZE41_17720 {ECO:0000313|EMBL:AMQ07624.1};
OS Sporosarcina psychrophila (Bacillus psychrophilus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1476 {ECO:0000313|EMBL:AMQ07624.1, ECO:0000313|Proteomes:UP000071057};
RN [1] {ECO:0000313|EMBL:AMQ07624.1, ECO:0000313|Proteomes:UP000071057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6497 {ECO:0000313|EMBL:AMQ07624.1,
RC ECO:0000313|Proteomes:UP000071057};
RA Yan W.;
RT "Complete genome sequence of the Sporosarcina psychrophila DSM6497, a
RT psychrophila Bacillus that can mediate the Ca2+ precipitation.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443}.
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DR EMBL; CP014616; AMQ07624.1; -; Genomic_DNA.
DR RefSeq; WP_067212229.1; NZ_CP014616.1.
DR AlphaFoldDB; A0A127W289; -.
DR STRING; 1476.AZE41_17720; -.
DR KEGG; spsy:AZE41_17720; -.
DR OrthoDB; 9801810at2; -.
DR Proteomes; UP000071057; Chromosome.
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; 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.
PE 3: Inferred from homology;
KW Nucleotidyltransferase {ECO:0000313|EMBL:AMQ07624.1};
KW Transferase {ECO:0000313|EMBL:AMQ07624.1}.
FT DOMAIN 20..216
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 368 AA; 41934 MW; AC57595EF5B968BA CRC64;
MNTMMGLINL EHEHHYFHEL TYFRSGATIP FAGRYRLIDF PLSNMGNSNV ESVAIFTRNK
YRSLMDHLQT GGSWEMDERN GGLFILPPDW NDPSDISKGD LSFFHNNRDY FARGKSSYVL
ISGSQFITNT DYQDAFKSHL ANKADVTLIT THIETLNTEH DSAFRIEADE DGWVTTITND
KQENDLFTGV YIINKDLLMT LVDQCIAHHQ DHFFVHGIKE NLATLKVQTY KNNGYGVFIN
SIESYYRHNM NLLSEENYKA LFYKLPFIRT KVGNQPPTKY RNEASVKKSI LANGCIIAGE
VEGSVLFRGV TIEEGATVKN SIIMQRCKIE AGVHLENVIL DKDVHVTANQ QLIGSKDKPY
VVAKRQVM
//
