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Succinate--CoA ligase [ADP-forming] subunit beta (EC 6 2 1 5) (Succinyl-CoA synthetase subunit beta) (SCS-beta)

 A0A0D6HLC6_ECOLX        Unreviewed;       389 AA.
A0A0D6HLC6;
27-MAY-2015, integrated into UniProtKB/TrEMBL.
27-MAY-2015, sequence version 1.
02-JUN-2021, entry version 59.
RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta {ECO:0000256|HAMAP-Rule:MF_00558};
EC=6.2.1.5 {ECO:0000256|HAMAP-Rule:MF_00558};
AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000256|HAMAP-Rule:MF_00558};
Short=SCS-beta {ECO:0000256|HAMAP-Rule:MF_00558};
Name=sucC {ECO:0000256|HAMAP-Rule:MF_00558, ECO:0000313|EMBL:HAH1048894.1};
Synonyms=sucC_1 {ECO:0000313|EMBL:STN17345.1},
sucC_2 {ECO:0000313|EMBL:AUG96044.1}, sucC_3 {ECO:0000313|EMBL:STP22821.1};
ORFNames=B6V57_23275 {ECO:0000313|EMBL:AWG09206.1},
BvCmsSIP024_01814 {ECO:0000313|EMBL:GDU86654.1},
C4K41_17080 {ECO:0000313|EMBL:PPE29088.1},
CT146_10615 {ECO:0000313|EMBL:PIM23464.1},
DNR41_16690 {ECO:0000313|EMBL:RAH21182.1},
DU333_20815 {ECO:0000313|EMBL:RRK90229.1},
DW236_20440 {ECO:0000313|EMBL:RHG95021.1},
E8P32_08130 {ECO:0000313|EMBL:THG86186.1},
EA239_14450 {ECO:0000313|EMBL:KAA2143659.1},
EA250_14950 {ECO:0000313|EMBL:KAA1837108.1},
ELT31_21655 {ECO:0000313|EMBL:TFS41213.1},
EPS94_15440 {ECO:0000313|EMBL:RXB45484.1},
FQU83_25215 {ECO:0000313|EMBL:QDX38807.1},
G4280_23120 {ECO:0000313|EMBL:QMX30950.1},
HHG54_001221 {ECO:0000313|EMBL:HAH1048894.1},
HHJ44_17590 {ECO:0000313|EMBL:QJS74760.1},
HJ411_002639 {ECO:0000313|EMBL:HAI8045334.1},
HJM41_003196 {ECO:0000313|EMBL:HAI3357726.1},
HJO02_003539 {ECO:0000313|EMBL:HAI4144034.1},
HJS12_002665 {ECO:0000313|EMBL:HAI5400048.1},
HJS53_003445 {ECO:0000313|EMBL:HAI5448936.1},
HmCmsJML146_04319 {ECO:0000313|EMBL:GDA25107.1},
HPE52_20015 {ECO:0000313|EMBL:QKM88085.1},
HV055_22995 {ECO:0000313|EMBL:QMA04914.1},
HV348_23035 {ECO:0000313|EMBL:QLR35376.1},
MS8345_04528 {ECO:0000313|EMBL:AUG96044.1},
NCTC9075_06321 {ECO:0000313|EMBL:STP22821.1},
NCTC9434_02070 {ECO:0000313|EMBL:STN17345.1};
Escherichia coli.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=562 {ECO:0000313|EMBL:RHG95021.1, ECO:0000313|Proteomes:UP000284643};
[1] {ECO:0000313|EMBL:AWG09206.1, ECO:0000313|Proteomes:UP000324147}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ZJ3920 {ECO:0000313|EMBL:AWG09206.1,
ECO:0000313|Proteomes:UP000324147};
Shen Z., Wu Z., Wang Y., Shen Y.;
"Whole genome analysis revealed super genetic diversity of mcr-1 positive
E. coli strains from one hospital.";
Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:PIM23464.1, ECO:0000313|Proteomes:UP000229602}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ABU 91 {ECO:0000313|EMBL:PIM23464.1,
ECO:0000313|Proteomes:UP000229602};
Stork C., Kovacs B., Trost E., Kovacs T., Schneider G., Rozsai B.,
Kerenyi M., Emody L., Dobrindt U.;
"Whole-genome draft sequences of nine asymptomatic Escherichia coli
bacteriuria isolates from diabetic patients.";
Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:AUG96044.1, ECO:0000313|Proteomes:UP000233584}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MS8345 {ECO:0000313|EMBL:AUG96044.1,
ECO:0000313|Proteomes:UP000233584};
Forde B.M., Zowawi H.M., Harris P., Roberts L., Ibrahim E., Shaikh N.,
Deshmukh A., Al Maslamani M., Cottrell K., Trembizki E., Sundac L., Yu H.,
Li J., Schembri M.A., Whiley D., Paterson D.L., Beatson S.A.;
"Mcr-1 mediated colistin resistant Escherichia coli ST95 from Qatar.";
Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|Proteomes:UP000530279, ECO:0000313|Proteomes:UP000531585}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AMC_124 {ECO:0000313|EMBL:HAI3357726.1},
AMC_222 {ECO:0000313|EMBL:HAI5400048.1},
AMC_373 {ECO:0000313|EMBL:HAI5448936.1},
AMC_862 {ECO:0000313|EMBL:HAI4144034.1},
KOr015 {ECO:0000313|EMBL:HAH1048894.1, ECO:0000313|Proteomes:UP000531923},
and UPEC {ECO:0000313|EMBL:HAI8045334.1,
ECO:0000313|Proteomes:UP000586631};
PubMed=30286803;
Souvorov A., Agarwala R., Lipman D.J.;
"SKESA: strategic k-mer extension for scrupulous assemblies.";
Genome Biol. 19:153-150(2018).
[5] {ECO:0000313|EMBL:PPE29088.1, ECO:0000313|Proteomes:UP000238807}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DP254 {ECO:0000313|EMBL:PPE29088.1,
ECO:0000313|Proteomes:UP000238807};
Xu A., Johnson J.R., Sheen S., Sommers C.H.;
"Draft Genomic Sequencing Of Potential Extraintestinal Pathogenic
Escherichia coli DP254 Isolated From Retail Chicken Meat.";
Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000313|Proteomes:UP000303763, ECO:0000313|Proteomes:UP000304638}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=JML146 {ECO:0000313|EMBL:GDA25107.1,
ECO:0000313|Proteomes:UP000304638}, and
SI-P024 {ECO:0000313|EMBL:GDU86654.1, ECO:0000313|Proteomes:UP000303763};
Arimizu Y., Ogura Y.;
"Large scale genomics of bovine and human commensal E. coli to reveal the
emerging process of EHEC.";
Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000313|EMBL:RAH21182.1, ECO:0000313|Proteomes:UP000249503}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CG1MAC {ECO:0000313|EMBL:RAH21182.1,
ECO:0000313|Proteomes:UP000249503};
Fang X.;
"Metagenomics-based, strain-level analysis of E. coli from a time-series of
microbiome samples from a Crohns disease patient.";
Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
[8] {ECO:0000313|Proteomes:UP000254181, ECO:0000313|Proteomes:UP000254730}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCTC9075 {ECO:0000313|EMBL:STP22821.1,
ECO:0000313|Proteomes:UP000254181}, and
NCTC9434 {ECO:0000313|EMBL:STN17345.1, ECO:0000313|Proteomes:UP000254730};
Pathogen Informatics;
Doyle S.;
Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
[9] {ECO:0000313|EMBL:RHG95021.1, ECO:0000313|Proteomes:UP000284643}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AM20-38 {ECO:0000313|EMBL:RHG95021.1,
ECO:0000313|Proteomes:UP000284643};
Zou Y., Xue W., Luo G.;
"A genome reference for cultivated species of the human gut microbiota.";
Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
[10] {ECO:0000313|Proteomes:UP000408798, ECO:0000313|Proteomes:UP000478303}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=EC152_ST95C {ECO:0000313|EMBL:KAA2143659.1,
ECO:0000313|Proteomes:UP000478303}, and
EC68_ST95C {ECO:0000313|EMBL:KAA1837108.1,
ECO:0000313|Proteomes:UP000408798};
Hastak P., Myers G., Djordjevic S., Chowdhury P.R.;
"Genomic surveillance of multi-drug resistant E. coli causing blood-stream
infections.";
Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
[11] {ECO:0000313|EMBL:RRK90229.1, ECO:0000313|Proteomes:UP000272659}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=UMB6454 {ECO:0000313|EMBL:RRK90229.1,
ECO:0000313|Proteomes:UP000272659};
Garretto A., Miller-Ensminger T., Wolfe A.J., Putonti C.;
"E. coli isolates of the female bladder.";
Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
[12] {ECO:0000313|EMBL:RXB45484.1, ECO:0000313|Proteomes:UP000290055}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=46_rectal {ECO:0000313|EMBL:RXB45484.1,
ECO:0000313|Proteomes:UP000290055};
Potter R., Zou Z., Henderson J., Dantas G.;
"Genomic analysis of febrile catheter-associated UTI E. coli isolates.";
Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
[13] {ECO:0000313|EMBL:TFS41213.1, ECO:0000313|Proteomes:UP000315045}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=URMC_12 {ECO:0000313|EMBL:TFS41213.1,
ECO:0000313|Proteomes:UP000315045};
Mostafa H., Pecora N.;
"ESBL Survelliance.";
Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
[14] {ECO:0000313|EMBL:THG86186.1, ECO:0000313|Proteomes:UP000305235}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=E692 {ECO:0000313|EMBL:THG86186.1,
ECO:0000313|Proteomes:UP000305235};
Yu Y., Song W., Lau S.;
"Transcriptomic analysis of wild-type E.coli in M9-glucose medium and pore
water from marine sediment.";
Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
[15] {ECO:0000313|EMBL:QDX38807.1, ECO:0000313|Proteomes:UP000315141}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PU-1 {ECO:0000313|EMBL:QDX38807.1,
ECO:0000313|Proteomes:UP000315141};
Ma J., Yao H.;
"Extracellular polysaccharide and nucleotide biosynthesis is required for
optimal growth of porcine extraintestinal pathogenic Escherichia coli in
swine blood.";
Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
[16] {ECO:0000313|EMBL:QMX30950.1}
NUCLEOTIDE SEQUENCE.
STRAIN=78-Pyelo {ECO:0000313|EMBL:QMX30950.1};
PubMed=33235212;
Biggel M., Xavier B.B., Johnson J.R., Nielsen K.L., Frimodt-Moller N.,
Matheeussen V., Goossens H., Moons P., Van Puyvelde S.;
"Horizontally acquired papGII-containing pathogenicity islands underlie the
emergence of invasive uropathogenic Escherichia coli lineages.";
Nat. Commun. 11:5968-5968(2020).
[17] {ECO:0000313|Proteomes:UP000515709}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=78-Pyelo {ECO:0000313|Proteomes:UP000515709};
Biggel M.;
"Comparative genomics of urinary Escherichia coli isolates associated with
different clinical phenotypes.";
Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
[18] {ECO:0000313|EMBL:HAI3357726.1}
NUCLEOTIDE SEQUENCE.
STRAIN=AMC_124 {ECO:0000313|EMBL:HAI3357726.1},
AMC_222 {ECO:0000313|EMBL:HAI5400048.1},
AMC_373 {ECO:0000313|EMBL:HAI5448936.1},
AMC_862 {ECO:0000313|EMBL:HAI4144034.1},
KOr015 {ECO:0000313|EMBL:HAH1048894.1}, and
UPEC {ECO:0000313|EMBL:HAI8045334.1};
NCBI Pathogen Detection Project;
Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
[19] {ECO:0000313|EMBL:QJS74760.1, ECO:0000313|Proteomes:UP000501919}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SCU-306 {ECO:0000313|EMBL:QJS74760.1,
ECO:0000313|Proteomes:UP000501919};
Stephens C., Arismendi T., Wright M., Gonzalez A., Gill M., Hartman A.,
Pandori M., Hess D.;
"F plasmids are the primary drivers of antibiotic resistance in human-
associated commensal E. coli.";
Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
[20] {ECO:0000313|EMBL:QKM88085.1, ECO:0000313|Proteomes:UP000503101}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SCU-176 {ECO:0000313|EMBL:QKM88085.1,
ECO:0000313|Proteomes:UP000503101};
Stephens C., Arismendi T., Wright M., Hartman A., Gonzalez A., Gill M.,
Pandori M., Hess D.;
"Title: F plasmids are the major carriers of antibiotic resistance genes in
human-associated commensal E. coli.";
Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
[21] {ECO:0000313|Proteomes:UP000512389, ECO:0000313|Proteomes:UP000512432}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RHBSTW-00072 {ECO:0000313|EMBL:QMA04914.1,
ECO:0000313|Proteomes:UP000512389}, and
RHBSTW-01004 {ECO:0000313|EMBL:QLR35376.1,
ECO:0000313|Proteomes:UP000512432};
Shaw L.P.;
"REHAB project genomes.";
Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
(TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of
either ATP or GTP and thus represents the only step of substrate-level
phosphorylation in the TCA. The beta subunit provides nucleotide
specificity of the enzyme and binds the substrate succinate, while the
binding sites for coenzyme A and phosphate are found in the alpha
subunit. {ECO:0000256|HAMAP-Rule:MF_00558}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA;
Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000256|HAMAP-
Rule:MF_00558};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00558};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00558};
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
from succinyl-CoA (ligase route): step 1/1. {ECO:0000256|HAMAP-
Rule:MF_00558}.
-!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
{ECO:0000256|HAMAP-Rule:MF_00558}.
-!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
family. {ECO:0000256|HAMAP-Rule:MF_00558}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation of
feature annotation. {ECO:0000256|HAMAP-Rule:MF_00558}.
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EMBL; CP025401; AUG96044.1; -; Genomic_DNA.
EMBL; CP020545; AWG09206.1; -; Genomic_DNA.
EMBL; BFRA01000141; GDA25107.1; -; Genomic_DNA.
EMBL; BGIK01000009; GDU86654.1; -; Genomic_DNA.
EMBL; DABAIH010000006; HAH1048894.1; -; Genomic_DNA.
EMBL; DABEBS010000010; HAI3357726.1; -; Genomic_DNA.
EMBL; DABEHY010000010; HAI4144034.1; -; Genomic_DNA.
EMBL; DABERY010000011; HAI5400048.1; -; Genomic_DNA.
EMBL; DABESK010000010; HAI5448936.1; -; Genomic_DNA.
EMBL; DABFNC010000009; HAI8045334.1; -; Genomic_DNA.
EMBL; REBD01000012; KAA1837108.1; -; Genomic_DNA.
EMBL; RDVP01000009; KAA2143659.1; -; Genomic_DNA.
EMBL; PENJ01000005; PIM23464.1; -; Genomic_DNA.
EMBL; PSNQ01000014; PPE29088.1; -; Genomic_DNA.
EMBL; CP042246; QDX38807.1; -; Genomic_DNA.
EMBL; CP053231; QJS74760.1; -; Genomic_DNA.
EMBL; CP054345; QKM88085.1; -; Genomic_DNA.
EMBL; CP056190; QLR35376.1; -; Genomic_DNA.
EMBL; CP056876; QMA04914.1; -; Genomic_DNA.
EMBL; CP048867; QMX30950.1; -; Genomic_DNA.
EMBL; QLAC01000010; RAH21182.1; -; Genomic_DNA.
EMBL; QRIX01000014; RHG95021.1; -; Genomic_DNA.
EMBL; RRUU01000010; RRK90229.1; -; Genomic_DNA.
EMBL; SCIX01000011; RXB45484.1; -; Genomic_DNA.
EMBL; UGFV01000001; STN17345.1; -; Genomic_DNA.
EMBL; UGEM01000004; STP22821.1; -; Genomic_DNA.
EMBL; RZAR01000018; TFS41213.1; -; Genomic_DNA.
EMBL; SSTR01000008; THG86186.1; -; Genomic_DNA.
RefSeq; WP_001048629.1; NZ_WVVR01000009.1.
EnsemblBacteria; AUG96044; AUG96044; MS8345_04528.
EnsemblBacteria; PIM23464; PIM23464; CT146_10615.
EnsemblBacteria; PND96092; PND96092; C1I57_26330.
EnsemblBacteria; PPE29088; PPE29088; C4K41_17080.
EnsemblBacteria; RAH21182; RAH21182; DNR41_16690.
EnsemblBacteria; RIC99900; RIC99900; D1900_24530.
EnsemblBacteria; STN17345; STN17345; NCTC9434_02070.
EnsemblBacteria; STP22821; STP22821; NCTC9075_06321.
UniPathway; UPA00223; UER00999.
Proteomes; UP000229602; Unassembled WGS sequence.
Proteomes; UP000233584; Chromosome.
Proteomes; UP000238807; Unassembled WGS sequence.
Proteomes; UP000249503; Unassembled WGS sequence.
Proteomes; UP000254181; Unassembled WGS sequence.
Proteomes; UP000254730; Unassembled WGS sequence.
Proteomes; UP000272659; Unassembled WGS sequence.
Proteomes; UP000284643; Unassembled WGS sequence.
Proteomes; UP000290055; Unassembled WGS sequence.
Proteomes; UP000303763; Unassembled WGS sequence.
Proteomes; UP000304638; Unassembled WGS sequence.
Proteomes; UP000305235; Unassembled WGS sequence.
Proteomes; UP000315045; Unassembled WGS sequence.
Proteomes; UP000315141; Chromosome.
Proteomes; UP000324147; Chromosome.
Proteomes; UP000408798; Unassembled WGS sequence.
Proteomes; UP000478303; Unassembled WGS sequence.
Proteomes; UP000501919; Chromosome.
Proteomes; UP000503101; Chromosome.
Proteomes; UP000512389; Chromosome.
Proteomes; UP000512432; Chromosome.
Proteomes; UP000515709; Chromosome.
Proteomes; UP000530279; Unassembled WGS sequence.
Proteomes; UP000531585; Unassembled WGS sequence.
Proteomes; UP000531923; Unassembled WGS sequence.
Proteomes; UP000535533; Unassembled WGS sequence.
Proteomes; UP000558557; Unassembled WGS sequence.
Proteomes; UP000586631; Unassembled WGS sequence.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-UniRule.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
Gene3D; 3.30.1490.20; -; 1.
Gene3D; 3.40.50.261; -; 1.
HAMAP; MF_00558; Succ_CoA_beta; 1.
InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR005811; CoA_ligase.
InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
InterPro; IPR005809; Succ_CoA_synthase_bsu.
InterPro; IPR016102; Succinyl-CoA_synth-like.
PANTHER; PTHR11815; PTHR11815; 1.
Pfam; PF08442; ATP-grasp_2; 1.
Pfam; PF00549; Ligase_CoA; 1.
PIRSF; PIRSF001554; SucCS_beta; 1.
SUPFAM; SSF52210; SSF52210; 1.
TIGRFAMs; TIGR01016; sucCoAbeta; 1.
PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00558};
Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00558};
Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00558};
Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
Rule:MF_00558}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00558};
Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
Rule:MF_00558}.
DOMAIN 2..205
/note="ATP-grasp_2"
/evidence="ECO:0000259|Pfam:PF08442"
DOMAIN 265..383
/note="Ligase_CoA"
/evidence="ECO:0000259|Pfam:PF00549"
NP_BIND 55..57
/note="ATP"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
REGION 324..326
/note="Substrate binding; shared with subunit alpha"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
METAL 202
/note="Magnesium"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
METAL 216
/note="Magnesium"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
BINDING 48
/note="ATP"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
BINDING 104
/note="ATP; via amide nitrogen"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
BINDING 110
/note="ATP"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
BINDING 267
/note="Substrate; shared with subunit alpha"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
SEQUENCE 389 AA; 42378 MW; D399BDB3DCEE03B4 CRC64;
MNLHEYQAKS LLAGMGMPCP KEIAIQQISQ LADAWQHIAC PSKGAVLKAQ VHAGGRGKAG
GVKVLKQLPE AQAFVQQMLG SQLVTYQTGP EGQYVSSILL CENIYPVRQE LYFGMVVDRE
SQRVTFIVSP EGGVEIEKVA HETPEKISSV SIDPLTGVQP CHIREMFAVL QLEHGLFATF
SRLVNQAWKA FNELDFALLE INPLVLRETG EFMCADAKVS LDDNALYRHP ELQVLRDETQ
EDPRESQAAK LDLNYVSLDG NIGCMVNGAG LAMATMDIIK LYGEQPANFL DVGGGATQER
VSEAFRLIVS DSKVKAILVN IFGGIVRCDM IARAIIHALN EARITLPVVV RLSGNNAAEG
QRLLAESGLT VEAVNSLDDA AKRIIALLN


Related products :

Catalog number Product name Quantity
EIAAB40523 GTP-specific succinyl-CoA synthetase subunit beta,Homo sapiens,Human,SCS-betaG,Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial,Succinyl-CoA synthetase beta-G chain,SUCLG2
EIAAB40524 Bos taurus,Bovine,GTP-specific succinyl-CoA synthetase subunit beta,SCS-betaG,Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial,Succinyl-CoA synthetase beta-G chain,SUCLG2
EIAAB40522 ATP-specific succinyl-CoA synthetase subunit beta,Bos taurus,Bovine,SCS-betaA,Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial,Succinyl-CoA synthetase beta-A chain,SUCLA2
EIAAB40518 ATP-specific succinyl-CoA synthetase subunit beta,Mouse,Mus musculus,SCS-betaA,Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial,Succinyl-CoA synthetase beta-A chain,Sucla2
EIAAB40525 GTP-specific succinyl-CoA synthetase subunit beta,Mouse,Mus musculus,SCS-betaG,Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial,Succinyl-CoA synthetase beta-G chain,Suclg2
EIAAB40526 GTP-specific succinyl-CoA synthetase subunit beta,Pig,SCS-betaG,Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial,Succinyl-CoA synthetase beta-G chain,SUCLG2,Sus scrofa
EIAAB40519 ATP-specific succinyl-CoA synthetase subunit beta,Pig,SCS-betaA,Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial,Succinyl-CoA synthetase beta-A chain,SUCLA2,Sus scrofa
EIAAB40520 ATP-specific succinyl-CoA synthetase subunit beta,Homo sapiens,Human,Renal carcinoma antigen NY-REN-39,SCS-betaA,Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial,Succinyl-CoA synthetase b
EIAAB40521 ATP-specific succinyl-CoA synthetase subunit beta,Canis familiaris,Canis lupus familiaris,Dog,SCS-betaA,Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial,Succinyl-CoA synthetase beta-A cha
E12273m Pig ELISA Kit FOR Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial 96T
E1848m Mouse ELISA Kit FOR Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial 96T
CSB-EL022917DO Dog Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial(SUCLA2) ELISA kit 96T
H3517 Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial (SUCLA2), Dog, ELISA Kit 96T
H3529 Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial (SUCLG2), Pig, ELISA Kit 96T
H3520 Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial (SUCLA2), Pig, ELISA Kit 96T
H3519 Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial (SUCLA2), Mouse, ELISA Kit 96T
H3518 Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial (SUCLA2), Human, ELISA Kit 96T
H3526 Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial (SUCLG2), Bovine, ELISA Kit 96T
H3516 Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial (SUCLA2), Bovine, ELISA Kit 96T
CSB-EL022917MO Mouse Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial(SUCLA2) ELISA kit 96T
CSB-EL022920HU Human Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial(SUCLG2) ELISA kit 96T
CSB-EL022920MO Mouse Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial(SUCLG2) ELISA kit 96T
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CSB-EL022917BO Bovine Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial(SUCLA2) ELISA kit 96T
CSB-EL022920BO Bovine Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial(SUCLG2) ELISA kit 96T
Pathways :
WP1614: 1- and 2-Methylnaphthalene degradation
WP1655: Geraniol degradation
WP1566: Citrate cycle (TCA cycle)
WP1045: TGF-beta Receptor Signaling Pathway
WP209: Fatty Acid Beta Oxidation Meta
WP448: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1224: EBV LMP1 signaling
WP169: Fatty Acid Beta Oxidation 3
WP296: TCA Cycle - biocyc
WP1237: Fatty Acid Beta Oxidation
WP32: Translation Factors
WP809: TGF-beta Receptor Signaling Pathway
WP1058: Senescence and Autophagy
WP219: Cytoplasmic tRNA Synthetases
WP498: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1628: beta-Alanine metabolism
WP2218: sGC
WP506: Fatty Acid Beta Oxidation 1
WP1269: Fatty Acid Beta Oxidation
WP1722: Th1/Th2
WP368: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1106: Keap1-Nrf2
WP1897: Regulation of beta-cell development
WP401: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP930: TGF Beta Signaling Pathway

Related Genes :
[sucC b0728 JW0717] Succinate--CoA ligase [ADP-forming] subunit beta (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta) (SCS-beta)
[SUCLA2] Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (ATP-specific succinyl-CoA synthetase subunit beta) (A-SCS) (Succinyl-CoA synthetase beta-A chain) (SCS-betaA)
[sucD b0729 JW0718] Succinate--CoA ligase [ADP-forming] subunit alpha (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)
[SUCLG1] Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)
[SUCLG1] Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)
[Suclg1] Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)
[sucC scsB] Succinate--CoA ligase [GDP-forming] subunit beta (EC 6.2.1.4) (Succinyl-CoA synthetase subunit beta) (SCS-beta)
[sucC PA1588] Succinate--CoA ligase [ADP-forming] subunit beta (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta) (SCS-beta)
[scsA DDB_G0289325] Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha) (p36)
[] Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)
[Suclg1] Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)
[] Multifunctional fusion protein [Includes: Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (Succinyl-CoA synthetase beta chain) (SCS-beta); Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)]
[acdBI PF1787] Acetate--CoA ligase [ADP-forming] I subunit beta (EC 6.2.1.13) (ADP-forming acetyl coenzyme A synthetase I subunit beta) (ACS I subunit beta)
[Scsalpha1 Scsalpha CG1065] Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha) (Succinyl-coenzyme A synthetase alpha subunit 1)
[] Multifunctional fusion protein [Includes: Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (Succinyl-CoA synthetase beta chain) (SCS-beta); Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)]
[SUCLG1] Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha) (Fragment)
[tca-9 B9J10.140 NCU08471] Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (Succinyl-CoA synthetase beta chain) (SCS-beta)
[SUCLA2 QflA-11886] Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (ATP-specific succinyl-CoA synthetase subunit beta) (A-SCS) (Succinyl-CoA synthetase beta-A chain) (SCS-betaA)
[sucC BSU16090] Succinate--CoA ligase [ADP-forming] subunit beta (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta) (SCS-beta)
[acdAI PF1540] Acetate--CoA ligase [ADP-forming] I subunit alpha (EC 6.2.1.13) (ADP-forming acetyl coenzyme A synthetase I subunit alpha) (ACS I subunit alpha)
[sucD PA1589] Succinate--CoA ligase [ADP-forming] subunit alpha (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)
[NOO_LOCUS8770] Multifunctional fusion protein [Includes: Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (Succinyl-CoA synthetase beta chain) (SCS-beta); Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)]
[odhB sucC EPO11_04555] Succinate--CoA ligase [ADP-forming] subunit beta (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta) (SCS-beta)
[sucC sucD HWD61_08285] Multifunctional fusion protein [Includes: Succinate--CoA ligase [ADP-forming] subunit beta (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta) (SCS-beta); Succinate--CoA ligase [ADP-forming] subunit alpha (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)]
[sucD sucC KL86CIT2_200018] Multifunctional fusion protein [Includes: Succinate--CoA ligase [ADP-forming] subunit beta (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta) (SCS-beta); Succinate--CoA ligase [ADP-forming] subunit alpha (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)]
[sucC Rv0951 MTCY10D7.23c] Succinate--CoA ligase [ADP-forming] subunit beta (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta) (SCS-beta)
[sucC2 sucC SCO6585 SC8A6.06] Succinate--CoA ligase [ADP-forming] subunit beta 2 (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta 2) (SCS-beta 2)
[] Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)
[sucC RB10617] Succinate--CoA ligase [ADP-forming] subunit beta (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta) (SCS-beta)
[sucC sucD CMG10_01695] Multifunctional fusion protein [Includes: Succinate--CoA ligase [ADP-forming] subunit beta (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta) (SCS-beta); Succinate--CoA ligase [ADP-forming] subunit alpha (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)]

Bibliography :