ID A0A101WPI4_9FIRM Unreviewed; 372 AA.
AC A0A101WPI4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000313|EMBL:KUO76852.1};
GN ORFNames=APF77_21460 {ECO:0000313|EMBL:KUO76852.1};
OS Clostridia bacterium BRH_c25.
OC Bacteria; Bacillota; Clostridia.
OX NCBI_TaxID=1734399 {ECO:0000313|EMBL:KUO76852.1, ECO:0000313|Proteomes:UP000057710};
RN [1] {ECO:0000313|EMBL:KUO76852.1, ECO:0000313|Proteomes:UP000057710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c25 {ECO:0000313|EMBL:KUO76852.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUO76852.1}.
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DR EMBL; LOES01000027; KUO76852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101WPI4; -.
DR STRING; 1734399.APF77_21460; -.
DR Proteomes; UP000057710; Unassembled WGS sequence.
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:KUO76852.1};
KW Transferase {ECO:0000313|EMBL:KUO76852.1}.
FT DOMAIN 19..154
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 372 AA; 42413 MW; C173A2F991959D4D CRC64;
MLDYMGIVNL SEREDNIKEL TYHRPIASIP IAGRYRMIDF ALSNLVNSGI QNISIFTQHK
YRSLLDHLGT GKAWDLDRKN DGLFIMTPML NFYNMGISRG DIENFKNHID YIHLSKQNNV
IVTSSSMVCN LNYENAIKHH NETGADITVI YRRVGDCTED FQYCNILTVD EGGRITGVDL
NRGKESECNI SLDMFIMKKA LFLDIVNTCV SRGDCDYFKQ AVHNIVDKLK VYGYEFKGYL
ACVNSIHSYY KTNMQLLNLD TSKELFFRNG LIYTKVKDEP PTKYAENARV TNSLVANGCI
IDGQIENSII FRSVKVRKGA VVKNSILMQN CLIEEDVHLI NVILDKGVKV TRNKQLKGDE
SYPIVIEKKA II
//
