ID SUCC_PELPD Reviewed; 394 AA.
AC A1APQ8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 16-JAN-2019, entry version 77.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta {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 {ECO:0000255|HAMAP-Rule:MF_00558};
DE Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_00558};
GN Name=sucC {ECO:0000255|HAMAP-Rule:MF_00558};
GN OrderedLocusNames=Ppro_1716;
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Lovley D., Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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}.
DR EMBL; CP000482; ABK99328.1; -; Genomic_DNA.
DR RefSeq; WP_011735605.1; NC_008609.1.
DR ProteinModelPortal; A1APQ8; -.
DR SMR; A1APQ8; -.
DR STRING; 338966.Ppro_1716; -.
DR PRIDE; A1APQ8; -.
DR EnsemblBacteria; ABK99328; ABK99328; Ppro_1716.
DR KEGG; ppd:Ppro_1716; -.
DR eggNOG; ENOG4105CMV; Bacteria.
DR eggNOG; COG0045; LUCA.
DR HOGENOM; HOG000007059; -.
DR KO; K01903; -.
DR OMA; VQIEINP; -.
DR OrthoDB; 316012at2; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000006732; 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 1 394 Succinate--CoA ligase [ADP-forming]
FT subunit beta.
FT /FTId=PRO_1000082154.
FT DOMAIN 9 243 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_00558}.
FT NP_BIND 52 54 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT REGION 320 322 Substrate binding; shared with subunit
FT alpha. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT METAL 198 198 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_00558}.
FT METAL 212 212 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_00558}.
FT BINDING 45 45 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 98 98 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 101 101 ATP; via amide nitrogen.
FT {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 106 106 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 263 263 Substrate; shared with subunit alpha.
FT {ECO:0000255|HAMAP-Rule:MF_00558}.
SQ SEQUENCE 394 AA; 42653 MW; 985C8D0BF4590865 CRC64;
MKIHEYQAKD ILAGFGIAIP RGRVAMNASQ VERAARELGG HCVIKAQVYA GGRGKGGGIR
VAQDPGQAGE IAKELLGTKL VTPQTGPEGL EVRRLLVEEV VDIERELYLS ITLDRESSRY
CLIASAEGGM DIEEIARTAP DRIRILTIDP FIGLRSYQAR RTALGLGLVG PLCEECVELI
LNLYRCLLER DCSLVEINPL VVTNAGWLVA MDTKMTFDDN ALQRHCEYPD LVDYSQLNPL
EIAAARFDLS YIKLSGAIGC MVNGAGLAMA TLDVLKEAGG EPANFLDVGG GASREKVAEA
FRIILQDRDV RGVFVNIFGG IMRCDIIAQG IIDAASGGGC RLPIVVRMDG NRVEEGKQLL
RESGLNIRIG ENMGDGAQQI VAMLNREVNQ PCQS
//
