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Database: UniProt
Entry: O28732
LinkDB: O28732
Original site: O28732 
ID   SUCC1_ARCFU             Reviewed;         382 AA.
AC   O28732;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   16-JAN-2019, entry version 120.
DE   RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00558};
DE            Short=SCS-beta 1 {ECO:0000255|HAMAP-Rule:MF_00558};
GN   Name=sucC1 {ECO:0000255|HAMAP-Rule:MF_00558};
GN   OrderedLocusNames=AF_1540;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM
OS   9628 / NBRC 100126).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E.,
RA   Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D.,
RA   Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C.,
RA   Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G., Gill S.R.,
RA   Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J.,
RA   Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A.,
RA   Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A.,
RA   Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P.,
RA   Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C.,
RA   Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O.,
RA   Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-
RT   reducing archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
CC   -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid
CC       cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC       synthesis of either ATP or GTP and thus represents the only step
CC       of substrate-level phosphorylation in the TCA. The beta subunit
CC       provides nucleotide specificity of the enzyme and binds the
CC       substrate succinate, while the binding sites for coenzyme A and
CC       phosphate are found in the alpha subunit. {ECO:0000255|HAMAP-
CC       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-
CC       Rule:MF_00558};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000255|HAMAP-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
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_00558}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB89706.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE000782; AAB89706.1; ALT_INIT; Genomic_DNA.
DR   PIR; C69442; C69442.
DR   RefSeq; WP_048064709.1; NC_000917.1.
DR   ProteinModelPortal; O28732; -.
DR   SMR; O28732; -.
DR   STRING; 224325.AF1540; -.
DR   EnsemblBacteria; AAB89706; AAB89706; AF_1540.
DR   GeneID; 24795289; -.
DR   KEGG; afu:AF_1540; -.
DR   eggNOG; arCOG01337; Archaea.
DR   eggNOG; COG0045; LUCA.
DR   KO; K01903; -.
DR   OrthoDB; 72275at2157; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000002199; Chromosome.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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; Complete proteome; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN         1    382       Succinate--CoA ligase [ADP-forming]
FT                                subunit beta 1.
FT                                /FTId=PRO_0000102882.
FT   DOMAIN        9    235       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   NP_BIND      52     54       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   METAL       191    191       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   METAL       204    204       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   BINDING      45     45       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING      91     91       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING      94     94       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING      99     99       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   BINDING     255    255       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
SQ   SEQUENCE   382 AA;  42205 MW;  418ACBA41E64DA9F CRC64;
     MRLHEHQAKQ IFAKHGIRVP RGEVATSPEE AEKIAEKLGG RVVVKAQILV GGRGKAGGVK
     KANSPEEAKE VAKKILGMTI KGHRVEKVLV EEQLNMRKEY YVGYVVDKSS RLPTVIFSRM
     GGMDVEEIAA KHPDAIHRIY FDPLWGLKDY EVRKALFRAG FEGEEFKQMF DIIKKLVDIA
     FAYEAELTEI NPLAVTDEGF LAADARLNTD DNALYRHPEL AELREATEED PLEREARLKG
     INYVHLGGNV GVIANGAGLA MATMDIINLM GGKPANFLDT GGGLADPVKM KNCLLHVLKD
     PNVRVVFINI YAEITRCEKV AEGIILALDE APRKVPLVVK LAGTNEEIGR EMLERYSSEK
     GAEIHFVESI EEGARKAVEL AG
//
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