ID A0A0L8FPJ6_OCTBM Unreviewed; 456 AA.
AC A0A0L8FPJ6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03220};
DE EC=6.2.1.5 {ECO:0000256|HAMAP-Rule:MF_03220};
DE AltName: Full=ATP-specific succinyl-CoA synthetase subunit beta {ECO:0000256|HAMAP-Rule:MF_03220};
DE Short=A-SCS {ECO:0000256|HAMAP-Rule:MF_03220};
DE AltName: Full=Succinyl-CoA synthetase beta-A chain {ECO:0000256|HAMAP-Rule:MF_03220};
DE Short=SCS-betaA {ECO:0000256|HAMAP-Rule:MF_03220};
GN ORFNames=OCBIM_22012827mg {ECO:0000313|EMBL:KOF66315.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF66315.1};
RN [1] {ECO:0000313|EMBL:KOF66315.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF66315.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF66315.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-specific succinyl-CoA synthetase functions in the citric
CC acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC synthesis of ATP 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_03220}.
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_03220};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03220};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03220};
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_03220}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit
CC determines specificity for ATP. {ECO:0000256|HAMAP-Rule:MF_03220}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03220}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. ATP-specific subunit beta subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_03220}.
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DR EMBL; KQ428255; KOF66315.1; -; Genomic_DNA.
DR RefSeq; XP_014788228.1; XM_014932742.1.
DR AlphaFoldDB; A0A0L8FPJ6; -.
DR STRING; 37653.A0A0L8FPJ6; -.
DR EnsemblMetazoa; Ocbimv22012827m; Ocbimv22012827m.p; Ocbimv22012827m.g.
DR EnsemblMetazoa; XM_014932742.1; XP_014788228.1; LOC106882163.
DR GeneID; 106882163; -.
DR KEGG; obi:106882163; -.
DR OMA; ITACDEV; -.
DR OrthoDB; 1384037at2759; -.
DR UniPathway; UPA00223; UER00999.
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 HAMAP; MF_03220; Succ_CoA_betaA_euk; 1.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005811; CoA_ligase.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR034723; Succ_CoA_betaA_euk.
DR InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR NCBIfam; TIGR01016; sucCoAbeta; 1.
DR PANTHER; PTHR11815:SF1; 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; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03220};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03220};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03220};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03220};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03220};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03220}; Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_03220}.
FT DOMAIN 44..254
FT /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT /evidence="ECO:0000259|Pfam:PF08442"
FT DOMAIN 314..433
FT /note="ATP-citrate lyase/succinyl-CoA ligase"
FT /evidence="ECO:0000259|Pfam:PF00549"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220"
FT BINDING 98..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220"
FT BINDING 316
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220"
FT BINDING 373..375
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220"
FT SITE 87
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220"
FT SITE 155
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03220"
SQ SEQUENCE 456 AA; 49572 MW; AB8DDFB13F2FE606 CRC64;
MASFVLRSCL LQNGKFLKQD AKVLSSLLSL NLNPQSQQKR SLSLHEHLSF KLLEDGGVKV
PNFRVATTSE EAFKHAKDIA SETGNSDVVL KAQVLAGGRG RGEFESGLKG GVKLVYTAEE
ARKLAAQMIG SKLITKQTGA AGRICNSVMI CERLYSRREY YFAIAMERAY SGPVMVSSMQ
GGMAIEDVAR DNPDAIIKEP IDINTGLTKE QCLEMAKKLG MAGKSIEQVV DIMQKLYNVF
IKYDATMVEI NPLSEDSNGD VYCMDCKLNF DDNAAHRQKD IFAWKDWSQE DPRDHQAADA
DLNYIGLDGS IGCLVNGAGL AMATMDIIKL HGGNPANFLD VGGGATAKQV TEAFRLITSD
QNVQAILVNI FGGIMRCDVI AQGIIAAAAE LQLRIPIVVR LQGTRVEDAK ALIASSNLKI
LSCDNLDEAA KMIVKLSTIV GLAREAFVDV KFELPL
//