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GLGC_AGRFC
ID   GLGC_AGRFC              Reviewed;         420 AA.
AC   Q8U8L5;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=Atu4076;
GN   ORFNames=AGR_L_1560;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
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; AE007870; AAK89353.1; -; Genomic_DNA.
DR   PIR; AG3057; AG3057.
DR   PIR; G98228; G98228.
DR   RefSeq; NP_356568.1; NC_003063.2.
DR   RefSeq; WP_006313778.1; NC_003063.2.
DR   PDB; 6V96; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/T/V=1-420.
DR   PDB; 6V99; X-ray; 2.29 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/T/W=1-420.
DR   PDB; 6V9A; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/T/V=1-420.
DR   PDBsum; 6V96; -.
DR   PDBsum; 6V99; -.
DR   PDBsum; 6V9A; -.
DR   AlphaFoldDB; Q8U8L5; -.
DR   SMR; Q8U8L5; -.
DR   STRING; 176299.Atu4076; -.
DR   EnsemblBacteria; AAK89353; AAK89353; Atu4076.
DR   GeneID; 66224322; -.
DR   KEGG; atu:Atu4076; -.
DR   PATRIC; fig|176299.10.peg.3893; -.
DR   eggNOG; COG0448; Bacteria.
DR   HOGENOM; CLU_029499_14_1_5; -.
DR   OMA; QEWDVDE; -.
DR   PhylomeDB; Q8U8L5; -.
DR   BioCyc; AGRO:ATU4076-MON; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000813; Chromosome linear.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Carbohydrate metabolism; Glycogen biosynthesis;
KW   Glycogen metabolism; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..420
FT                   /note="Glucose-1-phosphate adenylyltransferase"
FT                   /id="PRO_0000195271"
FT   BINDING         107
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         172
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         187..188
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   BINDING         205
FT                   /ligand="alpha-D-glucose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58601"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00624"
FT   HELIX           9..12
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          13..19
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           24..30
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           48..56
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          61..66
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           71..80
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          91..97
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:6V99"
FT   HELIX           110..115
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           118..121
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           122..124
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          127..135
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           142..152
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          155..164
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           165..168
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          171..176
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          180..188
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          201..212
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           213..225
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   TURN            233..236
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           237..244
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          247..251
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           252..255
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           273..281
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           282..284
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          285..287
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          295..297
FT                   /evidence="ECO:0007829|PDB:6V99"
FT   STRAND          309..312
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          314..317
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          321..327
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          332..335
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          337..340
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          354..360
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          371..377
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          388..391
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           393..399
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          400..402
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   STRAND          408..410
FT                   /evidence="ECO:0007829|PDB:6V96"
FT   HELIX           412..416
FT                   /evidence="ECO:0007829|PDB:6V96"
SQ   SEQUENCE   420 AA;  47043 MW;  6F6BC076EFC27484 CRC64;
     MSEKRVQPLA RDAMAYVLAG GRGSRLKELT DRRAKPAVYF GGKARIIDFA LSNALNSGIR
     RIGVATQYKA HSLIRHLQRG WDFFRPERNE SFDILPASQR VSETQWYEGT ADAVYQNIDI
     IEPYAPEYMV ILAGDHIYKM DYEYMLQQHV DSGADVTIGC LEVPRMEATG FGVMHVNEKD
     EIIDFIEKPA DPPGIPGNEG FALASMGIYV FHTKFLMEAL RRDAADPTSS RDFGKDIIPY
     IVEHGKAVAH RFADSCVRSD FEHEPYWRDV GTIDAYWQAN IDLTDVVPDL DIYDKSWPIW
     TYAEITPPAK FVHDDEDRRG SAVSSVVSGD CIISGAALNR SLLFTGVRAN SYSRLENAVV
     LPSVKIGRHA QLSNVVIDHG VVIPEGLIVG EDPELDAKRF RRTESGICLI TQSMIDKLDL
 
 
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