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SUCC2_STRCO
ID   SUCC2_STRCO             Reviewed;         383 AA.
AC   O87840;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta 2 {ECO:0000255|HAMAP-Rule:MF_00558};
DE            EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_00558};
DE   AltName: Full=Succinyl-CoA synthetase subunit beta 2 {ECO:0000255|HAMAP-Rule:MF_00558};
DE            Short=SCS-beta 2 {ECO:0000255|HAMAP-Rule:MF_00558};
GN   Name=sucC2 {ECO:0000255|HAMAP-Rule:MF_00558}; Synonyms=sucC;
GN   OrderedLocusNames=SCO6585; ORFNames=SC8A6.06;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC       (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of
CC       either ATP or GTP and thus represents the only step of substrate-level
CC       phosphorylation in the TCA. The beta subunit provides nucleotide
CC       specificity of the enzyme and binds the substrate succinate, while the
CC       binding sites for coenzyme A and phosphate are found in the alpha
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_00558}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA;
CC         Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00558};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00558};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00558};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00558}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00558}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_00558}.
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DR   EMBL; AL939128; CAA19778.1; -; Genomic_DNA.
DR   PIR; T35773; T35773.
DR   RefSeq; NP_630664.1; NC_003888.3.
DR   RefSeq; WP_011031022.1; NZ_VNID01000002.1.
DR   AlphaFoldDB; O87840; -.
DR   SMR; O87840; -.
DR   STRING; 100226.SCO6585; -.
DR   GeneID; 1102024; -.
DR   KEGG; sco:SCO6585; -.
DR   PATRIC; fig|100226.15.peg.6690; -.
DR   eggNOG; COG0045; Bacteria.
DR   HOGENOM; CLU_037430_0_2_11; -.
DR   InParanoid; O87840; -.
DR   OMA; AIQQFKV; -.
DR   PhylomeDB; O87840; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0042709; C:succinate-CoA ligase complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IBA:GO_Central.
DR   GO; GO:0006104; P:succinyl-CoA metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.261; -; 1.
DR   HAMAP; MF_00558; Succ_CoA_beta; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR   InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR11815; PTHR11815; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001554; SucCS_beta; 1.
DR   SUPFAM; SSF52210; SSF52210; 1.
DR   TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..383
FT                   /note="Succinate--CoA ligase [ADP-forming] subunit beta 2"
FT                   /id="PRO_0000102870"
FT   DOMAIN          9..231
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         52..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         187
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         308..310
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
SQ   SEQUENCE   383 AA;  40162 MW;  5A3D05C0FD11DD03 CRC64;
     MDLYEHQARE LFKEHGIVVP RAEVTDSPER AREIARALGG RAVVKAQVKT GGRGKAGGVR
     LAADPAEAEE AARHILGMDI RGHTVDTVML AEPCEIEREF YVSYVLDRAS GGFLAIASAE
     GGTEIEEVAA RRPEAVARIP VDPATGVHTA TAVRIADAAG LPPQTVDTLV RLWKVLVRED
     ALLVEVNPLV RTAEGRIVAL DGKVTLDDNA RFRQSRWGET RQEDADSLEA RAGAKGLNYV
     KLDGEVGVIG NGAGLVMSTL DVVAGCGARP ANFLDIGGGA SARVMADGLS VVLSDPDVRS
     VLVNVFGGIT ACDAVADGIV RALDEVRLTK PLVVRLDGNN AARGRALLDA RAHPLVEQAT
     TMDGAARRAA RLATAASTAG QAG
 
 
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