ID A0A0M4L9H8_9MICC Unreviewed; 389 AA.
AC A0A0M4L9H8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta {ECO:0000256|HAMAP-Rule:MF_00558};
DE EC=6.2.1.5 {ECO:0000256|HAMAP-Rule:MF_00558};
DE AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000256|HAMAP-Rule:MF_00558};
DE Short=SCS-beta {ECO:0000256|HAMAP-Rule:MF_00558};
GN Name=sucC {ECO:0000256|HAMAP-Rule:MF_00558};
GN ORFNames=AL755_04835 {ECO:0000313|EMBL:ALE04970.1};
OS Arthrobacter sp. ERGS1:01.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1704044 {ECO:0000313|EMBL:ALE04970.1, ECO:0000313|Proteomes:UP000060433};
RN [1] {ECO:0000313|EMBL:ALE04970.1, ECO:0000313|Proteomes:UP000060433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS1:01 {ECO:0000313|EMBL:ALE04970.1,
RC ECO:0000313|Proteomes:UP000060433};
RX PubMed=26415659; DOI=10.1016/j.jbiotec.2015.09.025;
RA Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT "Complete genome sequence of Arthrobacter sp. ERGS1:01, a putative novel
RT bacterium with prospective cold active industrial enzymes, isolated from
RT East Rathong glacier in India.";
RL J. Biotechnol. 214:139-140(2015).
RN [2] {ECO:0000313|Proteomes:UP000060433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS1:01 {ECO:0000313|Proteomes:UP000060433};
RA Kumar R., Swarnkar M.K., Singh A.K., Singh D.;
RT "Complete Genome Sequencing of Arthrobacter sp. ERGS1:01.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of
CC either ATP or GTP 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:0000256|HAMAP-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:0000256|HAMAP-
CC Rule:MF_00558};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + GTP + succinate = GDP + phosphate + succinyl-CoA;
CC Xref=Rhea:RHEA:22120, ChEBI:CHEBI:30031, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:58189; Evidence={ECO:0000256|HAMAP-Rule:MF_00558};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00558};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00558};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_00558}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00558}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. {ECO:0000256|HAMAP-Rule:MF_00558}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00558}.
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DR EMBL; CP012479; ALE04970.1; -; Genomic_DNA.
DR RefSeq; WP_054010032.1; NZ_CP012479.1.
DR AlphaFoldDB; A0A0M4L9H8; -.
DR STRING; 1704044.AL755_04835; -.
DR KEGG; are:AL755_04835; -.
DR PATRIC; fig|1704044.3.peg.172; -.
DR OrthoDB; 9802602at2; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000060433; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:RHEA.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 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; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR005809; Succ_CoA_ligase-like_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR NCBIfam; TIGR01016; sucCoAbeta; 1.
DR PANTHER; PTHR11815:SF10; SUCCINATE--COA LIGASE [ADP-FORMING] SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11815; SUCCINYL-COA SYNTHETASE BETA CHAIN; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001554; SucCS_beta; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00558, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00558};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00558};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00558};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00558}; Reference proteome {ECO:0000313|Proteomes:UP000060433};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00558}.
FT DOMAIN 9..241
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 52..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 205
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 256
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
FT BINDING 318..320
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00558"
SQ SEQUENCE 389 AA; 40207 MW; 9555A6633F0DC8FE CRC64;
MDLFEYQARD MFEAHGVPVL AGIIAHTPEE AKAAAEKIGG VTVVKAQVKV GGRGKAGGVK
VAKTADEAFE HASAILGMDI KGHTVHTVMI AQGADIAEEF YFSVLLDRAN RNYLAMCSVE
GGMEIEELAV ERPEALARVA VDPAVGIDAA KADEIVAAAG FNAELAPKVA AAIIKLWDVF
KKEDATLVEV NPLVRTGAGD IVALDGKVSL DENADFRHPH HLDLEDAAAA DPLEAKAKAA
DLNYVKLDGE VGVIGNGAGL VMSTLDVVAY AGENHGGVKP ANFLDIGGGA SAEVMAAGLD
VILNDPQVKS VFVNVFGGIT ACDAVAKGIV GALAELGSAA NKPLVVRLDG NNVEEGRRIL
NEANHPLVTL AATMDEGADK AAELANASK
//
