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Database: UniProt
Entry: Q55AI5
LinkDB: Q55AI5
Original site: Q55AI5 
ID   SUCB1_DICDI             Reviewed;         445 AA.
AC   Q55AI5; Q86AG1;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   05-DEC-2018, entry version 98.
DE   RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03220};
DE            EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_03220};
DE   AltName: Full=ATP-specific succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_03220};
DE            Short=A-SCS {ECO:0000255|HAMAP-Rule:MF_03220};
DE   AltName: Full=Succinyl-CoA synthetase beta-A chain {ECO:0000255|HAMAP-Rule:MF_03220};
DE            Short=SCS-betaA {ECO:0000255|HAMAP-Rule:MF_03220};
DE   Flags: Precursor;
GN   Name=scsC; Synonyms=sucla2; ORFNames=DDB_G0271842;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A.,
RA   Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G.,
RA   Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A.,
RA   Platzer M., Rosenthal A., Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: ATP-specific succinyl-CoA synthetase functions in the
CC       citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA
CC       to the synthesis of ATP and thus represents the only step of
CC       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_03220}.
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_03220};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03220};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_03220};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_03220}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta
CC       subunit determines specificity for ATP. {ECO:0000255|HAMAP-
CC       Rule:MF_03220}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-
CC       Rule:MF_03220}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family. ATP-specific subunit beta subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03220}.
DR   EMBL; AAFI02000006; EAL71611.1; -; Genomic_DNA.
DR   RefSeq; XP_645537.1; XM_640445.1.
DR   ProteinModelPortal; Q55AI5; -.
DR   SMR; Q55AI5; -.
DR   STRING; 44689.DDB0231357; -.
DR   PaxDb; Q55AI5; -.
DR   PRIDE; Q55AI5; -.
DR   EnsemblProtists; EAL71611; EAL71611; DDB_G0271842.
DR   GeneID; 8618166; -.
DR   KEGG; ddi:DDB_G0271842; -.
DR   dictyBase; DDB_G0271842; scsC.
DR   eggNOG; KOG2799; Eukaryota.
DR   eggNOG; COG0045; LUCA.
DR   InParanoid; Q55AI5; -.
DR   KO; K01900; -.
DR   OMA; LCMDAKF; -.
DR   PhylomeDB; Q55AI5; -.
DR   Reactome; R-DDI-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER00999.
DR   PRO; PR:Q55AI5; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   Proteomes; UP000002195; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
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   HAMAP; MF_03220; Succ_CoA_betaA_euk; 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; IPR034723; Succ_CoA_betaA_euk.
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   Mitochondrion; Nucleotide-binding; Reference proteome;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     17       Mitochondrion. {ECO:0000255|HAMAP-
FT                                Rule:MF_03220}.
FT   CHAIN        18    445       Succinate--CoA ligase [ADP-forming]
FT                                subunit beta, mitochondrial.
FT                                {ECO:0000255|HAMAP-Rule:MF_03220}.
FT                                /FTId=PRO_0000328365.
FT   DOMAIN       43    270       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_03220}.
FT   NP_BIND      87     89       ATP. {ECO:0000255|HAMAP-Rule:MF_03220}.
FT   REGION      362    364       Substrate binding; shared with subunit
FT                                alpha. {ECO:0000255|HAMAP-Rule:MF_03220}.
FT   METAL       240    240       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03220}.
FT   METAL       254    254       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_03220}.
FT   BINDING      80     80       ATP. {ECO:0000255|HAMAP-Rule:MF_03220}.
FT   BINDING     305    305       Substrate; shared with subunit alpha.
FT                                {ECO:0000255|HAMAP-Rule:MF_03220}.
FT   SITE         76     76       Important for substrate specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03220}.
FT   SITE        144    144       Important for substrate specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03220}.
SQ   SEQUENCE   445 AA;  48350 MW;  5AE4D11AB5A4D199 CRC64;
     MLSNIVKKTI QSSKNLKSLV LNKSTSSLVY QKRFLNVHEY QAQKMMKSYG INCPVGNVAE
     TPEEAEKIAE VMNTQDLVVK AQVLAGGRGK GIFTSGLKGG VQLCSSAEDV KKFASKMLGH
     TLVTKQTGED GKVVHQVYVT ERHFLRKEMY FAILMDRKAG GPVMVASPEG GVDIEGVARD
     NPSAIFKEPI DIMIGVQPEQ TKRLAEKLGF SKKNISMAQD QMKKLYDFFI KNDCTLVEIN
     PLAETASGDV LCMDAKLNFD DNAAFRHPDI FKLRDKSQED PREVKAAEFD LNYIGLDGNI
     GCLVNGAGLA MASMDIIKLY GGSPANFLDV GGGATQKQVT EAIKLISSDK KVKSILVNIF
     GGIMKCDVIA LGIIAALKEL SIATPLVVRL QGTNVEAAKK IMEDSGLRLI AADNLDDAAQ
     KSVRIAEIVS LAEKSDLEIS FKLPL
//
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