ID   SUCB1_CANLF             Reviewed;          20 AA.
AC   P99507;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial {ECO:0000250|UniProtKB:Q9YI37};
DE            EC=6.2.1.5 {ECO:0000250|UniProtKB:Q9YI37};
DE   AltName: Full=ATP-specific succinyl-CoA synthetase subunit beta {ECO:0000250|UniProtKB:Q9YI37};
DE            Short=A-SCS {ECO:0000250|UniProtKB:Q9YI37};
DE   AltName: Full=Succinyl-CoA synthetase beta-A chain {ECO:0000250|UniProtKB:Q9YI37};
DE            Short=SCS-betaA {ECO:0000250|UniProtKB:Q9YI37};
DE   Flags: Fragment;
GN   Name=SUCLA2 {ECO:0000250|UniProtKB:Q9YI37};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Heart;
RX   PubMed=9504812; DOI=10.1002/elps.1150181514;
RA   Dunn M.J., Corbett J.M., Wheeler C.H.;
RT   "HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog
RT   heart proteins.";
RL   Electrophoresis 18:2795-2802(1997).
CC   -!- FUNCTION: ATP-specific succinyl-CoA synthetase functions in the citric
CC       acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC       synthesis of ATP 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:0000250|UniProtKB:Q9YI37}.
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;
CC         Evidence={ECO:0000250|UniProtKB:Q9YI37};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000250|UniProtKB:Q9YI37}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit
CC       determines specificity for ATP. Interacts with ALAS2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9YI37}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9YI37}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC       family. ATP-specific subunit beta subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P99507; -.
DR   STRING; 9615.ENSCAFP00000006646; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Ligase; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..>20
FT                   /note="Succinate--CoA ligase [ADP-forming] subunit beta,
FT                   mitochondrial"
FT                   /id="PRO_0000102813"
FT   DOMAIN          8..>20
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2248 MW;  BE8AEFD54DBDAC2E CRC64;
     LSLHEYMSME LLQEAGVSIP