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Database: UniProt
Entry: A0A0G4IHQ4_PLABS
LinkDB: A0A0G4IHQ4_PLABS
Original site: A0A0G4IHQ4_PLABS 
ID   A0A0G4IHQ4_PLABS        Unreviewed;       583 AA.
AC   A0A0G4IHQ4;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Succinate-CoA ligase subunit beta {ECO:0000256|RuleBase:RU361258};
DE            EC=6.2.1.- {ECO:0000256|RuleBase:RU361258};
DE   Flags: Fragment;
GN   ORFNames=PBRA_000500 {ECO:0000313|EMBL:CEO94714.1};
OS   Plasmodiophora brassicae (Clubroot disease agent).
OC   Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC   Plasmodiophoridae; Plasmodiophora.
OX   NCBI_TaxID=37360 {ECO:0000313|EMBL:CEO94714.1, ECO:0000313|Proteomes:UP000039324};
RN   [1] {ECO:0000313|EMBL:CEO94714.1, ECO:0000313|Proteomes:UP000039324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3 {ECO:0000313|EMBL:CEO94714.1};
RA   Chooi Y.-H.;
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005064}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000256|RuleBase:RU361258}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC       family. {ECO:0000256|RuleBase:RU361258}.
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DR   EMBL; CDSF01000001; CEO94714.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4IHQ4; -.
DR   STRING; 37360.A0A0G4IHQ4; -.
DR   EnsemblProtists; CEO94714; CEO94714; PBRA_000500.
DR   OMA; CLQVEIN; -.
DR   OrthoDB; 1384037at2759; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000039324; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; 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   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU361258};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361258};
KW   Reference proteome {ECO:0000313|Proteomes:UP000039324}.
FT   DOMAIN          172..381
FT                   /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT                   /evidence="ECO:0000259|Pfam:PF08442"
FT   DOMAIN          441..561
FT                   /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00549"
FT   REGION          120..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CEO94714.1"
SQ   SEQUENCE   583 AA;  63374 MW;  6C38AA3E0DE7CB1E CRC64;
     LPSLYMVIVL QPPANACNSA LHDPRLAVEG YLHPVCTFKT VDGVVSSSPD AIRPSRIKVT
     QPERNLTGCT TCWLPIVRSG QHEESAKQVV GSSHKNASVW LSSGSGNCLA VCSLNFRSSK
     SGAGPGSGRS RHGWGGVHRR SRQMQRAAIR AGRWAVRVRP SQQSGAQVRF LNIHEYLSHD
     ILRKFSVPTA NGFPARTPEE AAEAARKIGG KDFVVKAQVL AGGRGKGRFT NGFEGGVHAA
     NSPGQVRDLA AKMLGQHLVT KQTDSKGRPV DIVYVVERLF IRRECYFAIL LDRSANGPVL
     VASPKGGMDI EKVAAETPDF IFKAAVDDLE AGPTDDQLST LAAGMGFSEE NSLDEAKKVM
     SSLYQLFRKT DATLVEINPL CETHDGRVRC TDAKLNFDDN AEYRQKEIFE LRDRKQEDPR
     EVMASEYGLN YIGLDGNIGC LVNGAGLAMA TMDIIKLQGG SPANFLDLGG GATERTVTKA
     FEILNMDQRV EAILVNIFGG IMKCDVIALG LIAAVTTTDM KKPLVVRLEG TNVDEAKKLI
     EDSGLRMMTC DDLEDAARKA VRVAEIVRMA RDVHIDVKFE LPL
//
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