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

 A0A521Y5S7_9GAMM        Unreviewed;       779 AA.
A0A521Y5S7;
16-OCT-2019, integrated into UniProtKB/TrEMBL.
16-OCT-2019, sequence version 1.
02-JUN-2021, entry version 7.
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=odhB {ECO:0000313|EMBL:TAK76215.1};
Synonyms=sucC {ECO:0000256|HAMAP-Rule:MF_00558};
ORFNames=EPO11_04555 {ECO:0000313|EMBL:TAK76215.1};
Gammaproteobacteria bacterium.
Bacteria; Proteobacteria; Gammaproteobacteria.
NCBI_TaxID=1913989 {ECO:0000313|EMBL:TAK76215.1, ECO:0000313|Proteomes:UP000318705};
[1] {ECO:0000313|EMBL:TAK76215.1, ECO:0000313|Proteomes:UP000318705}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FW301-02_bin.23 {ECO:0000313|EMBL:TAK76215.1};
Tian R., Ning D., He Z., Zhang P., Shi W., Wu L., Zhang Y., Yang Y.,
Arkin A., Matthew F., Hazen T., Stalh D., Alm E., Zhou J.;
"Small is mighty: adaptation of Patescibacteria to groundwater environment
leads to their genome simplicity.";
Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: E2 component of the 2-oxoglutarate dehydrogenase (OGDH)
complex which catalyzes the second step in the conversion of 2-
oxoglutarate to succinyl-CoA and CO(2). {ECO:0000256|ARBA:ARBA00004052,
ECO:0000256|RuleBase:RU361138}.
-!- 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=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase
complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-
succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex
component E2] + CoA; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581,
Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61;
Evidence={ECO:0000256|ARBA:ARBA00001267,
ECO:0000256|RuleBase:RU361138};
-!- 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=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
Evidence={ECO:0000256|ARBA:ARBA00001938};
-!- COFACTOR:
Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
Evidence={ECO:0000256|RuleBase:RU361138};
Note=Binds 1 lipoyl cofactor covalently.
{ECO:0000256|RuleBase:RU361138};
-!- 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: Amino-acid degradation. {ECO:0000256|ARBA:ARBA00005023}.
-!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
pathway; glutaryl-CoA from L-lysine: step 6/6.
{ECO:0000256|ARBA:ARBA00005145, ECO:0000256|RuleBase:RU361138}.
-!- 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 2-oxoacid dehydrogenase family.
{ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361138}.
-!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
family. {ECO:0000256|HAMAP-Rule:MF_00558}.
-!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
whole genome shotgun (WGS) entry which is preliminary data.
{ECO:0000313|EMBL:TAK76215.1}.
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EMBL; SCTP01000142; TAK76215.1; -; Genomic_DNA.
UniPathway; UPA00223; UER00999.
UniPathway; UPA00868; UER00840.
Proteomes; UP000318705; Unassembled WGS sequence.
GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; 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:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniRule.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
Gene3D; 3.30.1490.20; -; 1.
Gene3D; 3.30.559.10; -; 1.
Gene3D; 3.40.50.261; -; 1.
Gene3D; 4.10.320.10; -; 1.
HAMAP; MF_00558; Succ_CoA_beta; 1.
InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR000089; Biotin_lipoyl.
InterPro; IPR023213; CAT-like_dom_sf.
InterPro; IPR005811; CoA_ligase.
InterPro; IPR036625; E3-bd_dom_sf.
InterPro; IPR004167; PSBD.
InterPro; IPR011053; Single_hybrid_motif.
InterPro; IPR006255; SucB.
InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
InterPro; IPR005809; Succ_CoA_synthase_bsu.
InterPro; IPR016102; Succinyl-CoA_synth-like.
PANTHER; PTHR11815; PTHR11815; 1.
Pfam; PF00198; 2-oxoacid_dh; 1.
Pfam; PF08442; ATP-grasp_2; 1.
Pfam; PF00364; Biotin_lipoyl; 1.
Pfam; PF02817; E3_binding; 1.
Pfam; PF00549; Ligase_CoA; 1.
SUPFAM; SSF47005; SSF47005; 1.
SUPFAM; SSF51230; SSF51230; 1.
SUPFAM; SSF52210; SSF52210; 1.
TIGRFAMs; TIGR01347; sucB; 1.
TIGRFAMs; TIGR01016; sucCoAbeta; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PROSITE; PS51826; PSBD; 1.
PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
3: Inferred from homology;
Acyltransferase {ECO:0000256|RuleBase:RU361138,
ECO:0000313|EMBL:TAK76215.1};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00558, ECO:0000256|PROSITE-
ProRule:PRU00409};
Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00558};
Lipoyl {ECO:0000256|RuleBase:RU361138};
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, ECO:0000256|PROSITE-
ProRule:PRU00409};
Transferase {ECO:0000256|RuleBase:RU361138, ECO:0000313|EMBL:TAK76215.1};
Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
Rule:MF_00558}.
DOMAIN 2..77
/note="Lipoyl-binding"
/evidence="ECO:0000259|PROSITE:PS50968"
DOMAIN 100..137
/note="Peripheral subunit-binding (PSBD)"
/evidence="ECO:0000259|PROSITE:PS51826"
DOMAIN 395..615
/note="ATP-grasp"
/evidence="ECO:0000259|PROSITE:PS50975"
NP_BIND 439..441
/note="ATP"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
REGION 707..709
/note="Substrate binding; shared with subunit alpha"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
METAL 585
/note="Magnesium"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
METAL 599
/note="Magnesium"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
BINDING 432
/note="ATP"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
BINDING 485
/note="ATP"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
BINDING 488
/note="ATP; via amide nitrogen"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
BINDING 493
/note="ATP"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
BINDING 650
/note="Substrate; shared with subunit alpha"
/evidence="ECO:0000256|HAMAP-Rule:MF_00558"
SEQUENCE 779 AA; 84438 MW; F836FCF7D8717F17 CRC64;
MAIEVKVPLL PESVSDAVVS TWHKKVGDPI SQGENIVDLE TDKVMLEVPA PADGVLKEII
KQTGSTVHSE ELLAVIDTAA AASAKPAAVE QKPQVLQSVP ASPSARRVAA EHDVDVSQVS
GTGKGGRVMK ENVMSFLDNQ TPSVANVPVG ARPEKRVPMT RIRARIAERL LEVTQTTAML
TTFNEINMQH VIDLRNRYKE KFEKVHKVRL GFMSFFVKAC AEALKRSPVV NASLDGNDIV
YHGYYDIGVA VSTERGLVVP VLRDADQMSM AEIEAKIAEY AEKARAGKLS LEEMQGGTFS
ITNGGVFGSL MATPLLNSPQ CAILGMHKIQ ERPVAENGQV VIRPMMYVAL SYDHRLIDGK
ESVTFLVTIK ELLEDPTRLL LEVQPPMNLH EYQSKQLLAE YGLPVSRGEV AANVEQAVAI
ASTLSTPRWV VKAQVHAGGR GKAGGVKIVS TKEELAEVVR SLLGKHLVTY QTTAEGQPVN
QVLIEEPCDI ERELYLGAVI DRSKQRIVFM ASTEGGVEIE KVAEEHPEKI LTTVVDPLVG
VQPYQGRQLA FALGLKGEQI KQFVQLLMGL GKMFKESDLS LLEINPLVIT KQGQLLCLDA
KITIDDNALY RQPTLRAMRD ASQEDERENR ARDWELNYIA LDGDIGCMVN GAGLAMATMD
MIKLHGGNPA NFLDVGGGAT KERVSEAFKI ILSDTKVKAI LINIFGGIVR CDLIAEGIMG
AVAEVGTALP VVVRLEGNNA ELGAKMLNDS KKQGLNIIAA ESFTDAAKKV VQAAANVGV


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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 :