ID W9CB29_SCLBF Unreviewed; 445 AA.
AC W9CB29;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03219};
DE EC=6.2.1.5 {ECO:0000256|HAMAP-Rule:MF_03219};
DE AltName: Full=Succinyl-CoA synthetase beta chain {ECO:0000256|HAMAP-Rule:MF_03219};
DE Short=SCS-beta {ECO:0000256|HAMAP-Rule:MF_03219};
GN ORFNames=SBOR_7564 {ECO:0000313|EMBL:ESZ92064.1};
OS Sclerotinia borealis (strain F-4128).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=1432307 {ECO:0000313|EMBL:ESZ92064.1, ECO:0000313|Proteomes:UP000019487};
RN [1] {ECO:0000313|EMBL:ESZ92064.1, ECO:0000313|Proteomes:UP000019487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-4157 {ECO:0000313|Proteomes:UP000019487};
RX PubMed=24459262; DOI=10.1128/genomeA.01175-13;
RA Mardanov A.V., Beletsky A.V., Kadnikov V.V., Ignatov A.N., Ravin N.V.;
RT "Draft genome sequence of Sclerotinia borealis, a psychrophilic plant
RT pathogenic fungus.";
RL Genome Announc. 2:E0117513-E0117513(2014).
CC -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP
CC and thus represents the only step of substrate-level phosphorylation in
CC the TCA. The beta subunit provides nucleotide specificity of the enzyme
CC and binds the substrate succinate, while the binding sites for coenzyme
CC A and phosphate are found in the alpha subunit. {ECO:0000256|HAMAP-
CC Rule:MF_03219}.
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:0000256|ARBA:ARBA00043683, ECO:0000256|HAMAP-
CC Rule:MF_03219};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03219};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03219};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005064, ECO:0000256|HAMAP-Rule:MF_03219}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC {ECO:0000256|HAMAP-Rule:MF_03219, ECO:0000256|RuleBase:RU361258}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03219}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. {ECO:0000256|HAMAP-Rule:MF_03219,
CC ECO:0000256|RuleBase:RU361258}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESZ92064.1}.
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DR EMBL; AYSA01000428; ESZ92064.1; -; Genomic_DNA.
DR AlphaFoldDB; W9CB29; -.
DR STRING; 1432307.W9CB29; -.
DR HOGENOM; CLU_037430_0_0_1; -.
DR OrthoDB; 1384037at2759; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000019487; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; 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_03219, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03219};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03219};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03219}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03219};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03219}; Reference proteome {ECO:0000313|Proteomes:UP000019487};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_03219}.
FT DOMAIN 43..270
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT BINDING 87..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT BINDING 305
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
FT BINDING 362..364
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03219"
SQ SEQUENCE 445 AA; 47977 MW; 557DEDF3CA0D3496 CRC64;
MFKLARSQPL AAALKASRVS MPSRMVGAAQ QKRALSIHEY LSADLLRKYG IGVPNGFVAN
NADEAEAIAK KIGGDDMVIK AQVLAGGRGK GTFDNGLKGG VRVIYSPTEA KMFADQMIGH
KLVTKQTGAQ GRICNSVYIC ERKFARREFY LAILMDRGSQ GPVIVSSSQG GMDIEAVAKE
TPNAITTTYI DIHKGVTDDI ARKIVTDIGF SEQCIEDAKD TVQKLYKIFM EKDATQIEIN
PLSETSDHKV LAMDAKLGFD DNAEFRQKEV FEWRDTSQED ADEVRAAESG LNFIKLGGDI
GCLVNGAGLA MATMDIIKLN GGEPANFLDV GGGATPQAIK EAFTLITSDP KVTAIFVNIF
GGIVRCDAIA QGLISTVESM DLRIPIIARL QGTNMEAAHK LINEAGLKIF SIDDLQSAAE
KAVQFSKVVK MARDIDVGVE FSLGI
//
