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Database: UniProt
Entry: A0A0L8FPJ6_OCTBM
LinkDB: A0A0L8FPJ6_OCTBM
Original site: A0A0L8FPJ6_OCTBM 
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
//
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