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Database: UniProt
Entry: A0A2K5Y5L6_MANLE
LinkDB: A0A2K5Y5L6_MANLE
Original site: A0A2K5Y5L6_MANLE 
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
//
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