ID A0A2K5Y5L6_MANLE Unreviewed; 437 AA.
AC A0A2K5Y5L6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03221};
DE EC=6.2.1.4 {ECO:0000256|HAMAP-Rule:MF_03221};
DE AltName: Full=GTP-specific succinyl-CoA synthetase subunit beta {ECO:0000256|HAMAP-Rule:MF_03221};
DE Short=G-SCS {ECO:0000256|HAMAP-Rule:MF_03221};
DE Short=GTPSCS {ECO:0000256|HAMAP-Rule:MF_03221};
DE AltName: Full=Succinyl-CoA synthetase beta-G chain {ECO:0000256|HAMAP-Rule:MF_03221};
DE Short=SCS-betaG {ECO:0000256|HAMAP-Rule:MF_03221};
GN Name=SUCLG2 {ECO:0000256|HAMAP-Rule:MF_03221};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000010830.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000010830.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: GTP-specific succinyl-CoA synthetase functions in the citric
CC acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC synthesis of 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_03221}.
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; EC=6.2.1.4; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03221};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03221};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03221};
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_03221}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit
CC determines specificity for GTP. {ECO:0000256|HAMAP-Rule:MF_03221}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03221}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. GTP-specific subunit beta subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_03221}.
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DR AlphaFoldDB; A0A2K5Y5L6; -.
DR STRING; 9568.ENSMLEP00000010830; -.
DR Ensembl; ENSMLET00000034248.1; ENSMLEP00000010830.1; ENSMLEG00000029579.1.
DR GeneTree; ENSGT00390000010170; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP 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:UniProtKB-EC.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IEA:InterPro.
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_03221; Succ_CoA_betaG_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; IPR034722; Succ_CoA_betaG_euk.
DR InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR NCBIfam; TIGR01016; sucCoAbeta; 1.
DR PANTHER; PTHR11815:SF12; SUCCINATE--COA LIGASE [GDP-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 GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03221};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03221};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03221};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03221}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03221};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03221}; Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_03221}.
FT DOMAIN 39..245
FT /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT /evidence="ECO:0000259|Pfam:PF08442"
FT DOMAIN 307..417
FT /note="ATP-citrate lyase/succinyl-CoA ligase"
FT /evidence="ECO:0000259|Pfam:PF00549"
FT BINDING 57
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03221"
FT BINDING 90..92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03221"
FT BINDING 146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03221"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03221"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03221"
FT BINDING 308
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03221"
FT BINDING 365..367
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03221"
FT SITE 79
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03221"
FT SITE 147
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03221"
SQ SEQUENCE 437 AA; 47564 MW; 81E14F75280DC8F8 CRC64;
MASPVATQAG KLLRALALRP RFLAVGSQAV QLTSRRWLNL QEYQSKKLMS DNGVRVQRFF
VADTANEALE AAKRLNAKEI VLKAQILAGG RGKGVFNSGL KGGVHLTKDP NVVGQLAKQM
IGYNLATKQT PKEGVKVNKV MVAEALDISR ETYLAILMDR SCNGPVLVGS PQGGVDIEEV
AASNPELIFK EQIDIFEGIK DSQAQRMAEN LGFVGPLKSQ AADQITKLYN LFLKIDATQV
EVNPFGETPE GQVVCFDAKI NFDDNAEFRQ KDIFAMDDKS ENEPIENEAA KYDLKYIGLD
GNIACFVNGA GLAMATCDII FLNGGKPANF LDLGGGVKEA QVYQAFKLLT ADPKVEAILV
NIFGGIVNCA IIANGITKAC RELELKVPLV VRLEGTFMKK ESYMHIKQER GNSNGNITGI
QENVTHQNLS KCAISFF
//