GLGC_RHILO
ID GLGC_RHILO Reviewed; 421 AA.
AC Q985P3; Q93QE7;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00624};
DE EC=2.7.7.27 {ECO:0000255|HAMAP-Rule:MF_00624};
DE AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00624};
DE Short=ADPGlc PPase {ECO:0000255|HAMAP-Rule:MF_00624};
DE AltName: Full=ADP-glucose synthase {ECO:0000255|HAMAP-Rule:MF_00624};
GN Name=glgC {ECO:0000255|HAMAP-Rule:MF_00624}; OrderedLocusNames=mlr7588;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lepek V.C., Tomatis P.E., Giambiagi S., Ugalde R.A.;
RT "Partial characterization of R.loti gene cluster for glycogen metabolism:
RT differences with A.tumefaciens.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
CC -!- FUNCTION: Involved in the biosynthesis of ADP-glucose, a building block
CC required for the elongation reactions to produce glycogen. Catalyzes
CC the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to
CC produce pyrophosphate and ADP-Glc. {ECO:0000255|HAMAP-Rule:MF_00624}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose
CC + diphosphate; Xref=Rhea:RHEA:12120, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57498,
CC ChEBI:CHEBI:58601; EC=2.7.7.27; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00624};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00624}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00624}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000255|HAMAP-Rule:MF_00624}.
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DR EMBL; AF268969; AAK58595.1; -; Genomic_DNA.
DR EMBL; BA000012; BAB54019.1; -; Genomic_DNA.
DR RefSeq; WP_010914967.1; NC_002678.2.
DR AlphaFoldDB; Q985P3; -.
DR SMR; Q985P3; -.
DR STRING; 266835.14027065; -.
DR EnsemblBacteria; BAB54019; BAB54019; BAB54019.
DR GeneID; 66685156; -.
DR KEGG; mlo:mlr7588; -.
DR eggNOG; COG0448; Bacteria.
DR HOGENOM; CLU_029499_14_1_5; -.
DR OMA; QEWDVDE; -.
DR OrthoDB; 1557977at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_00624; GlgC; 1.
DR InterPro; IPR011831; ADP-Glc_PPase.
DR InterPro; IPR005836; ADP_Glu_pyroP_CS.
DR InterPro; IPR023049; GlgC_bac.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43523; PTHR43523; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR02091; glgC; 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; Carbohydrate metabolism; Glycogen biosynthesis;
KW Glycogen metabolism; Nucleotide-binding; Nucleotidyltransferase;
KW Transferase.
FT CHAIN 1..421
FT /note="Glucose-1-phosphate adenylyltransferase"
FT /id="PRO_0000195317"
FT BINDING 108
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 173
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 188..189
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT BINDING 206
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT CONFLICT 145
FT /note="M -> L (in Ref. 1; AAK58595)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="N -> G (in Ref. 1; AAK58595)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="D -> E (in Ref. 1; AAK58595)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="E -> D (in Ref. 1; AAK58595)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="A -> M (in Ref. 1; AAK58595)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="I -> V (in Ref. 1; AAK58595)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="T -> S (in Ref. 1; AAK58595)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="T -> A (in Ref. 1; AAK58595)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="A -> V (in Ref. 1; AAK58595)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="I -> V (in Ref. 1; AAK58595)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 47037 MW; 6DD17FC327A876D9 CRC64;
MADLKRTQPL ARDAMAYVLA GGRGSRLKEL TDRRAKPAVY FGGKTRIIDF ALSNALNSGI
RRLGVATQYK AHSLIRHLQR GWNFLRPERN ESFDILPASQ RVSETQWYEG TADAVYQNID
IIEAYGPEYM VILAGDHIYK MDYEMMLRQH VDANADVTVG CLEVPRMEAT GFGVMHVDAK
DNIIAFVEKP ADPPGIPGNP DFALASMGIY VFKTKFLMEQ LRRDAAEPGS SRDFGKDIIP
YIVQHGKAIA HRFTKSCVRS TAENEAYWRD VGTVDAYWEA NIDLTDITPE LDLYDRDWPI
WTYAELKPPA KFVHDEDGRR GSAVSSLVSG DCIVSGATLK KSLIFTGARI NSYSTLEEVV
MLPDVHVGRN AKLKRVVIDH GVRIPEGLVV GEDPALDAKR FRVSEKGICL ITQDMINKLG
L
