SUCB2_PIG
ID SUCB2_PIG Reviewed; 433 AA.
AC P53590; Q95279;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03221};
DE EC=6.2.1.4 {ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000269|PubMed:27487822, ECO:0000269|PubMed:8401211};
DE AltName: Full=GTP-specific succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_03221};
DE Short=G-SCS {ECO:0000255|HAMAP-Rule:MF_03221};
DE Short=GTPSCS {ECO:0000255|HAMAP-Rule:MF_03221};
DE AltName: Full=Succinyl-CoA synthetase beta-G chain {ECO:0000255|HAMAP-Rule:MF_03221};
DE Short=SCS-betaG {ECO:0000255|HAMAP-Rule:MF_03221};
DE Flags: Precursor; Fragment;
GN Name=SUCLG2 {ECO:0000255|HAMAP-Rule:MF_03221};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-41, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC TISSUE=Heart;
RX PubMed=8401211; DOI=10.1002/pro.5560020808;
RA Bailey D.L., Wolodko W.T., Bridger W.A.;
RT "Cloning, characterization, and expression of the beta subunit of pig heart
RT succinyl-CoA synthetase.";
RL Protein Sci. 2:1255-1262(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-82.
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 39-433 IN COMPLEX WITH SUCLG1.
RX PubMed=10873456; DOI=10.1006/jmbi.2000.3807;
RA Fraser M.E., James M.N., Bridger W.A., Wolodko W.T.;
RT "Phosphorylated and dephosphorylated structures of pig heart, GTP-specific
RT succinyl-CoA synthetase.";
RL J. Mol. Biol. 299:1325-1339(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 40-433 IN COMPLEX WITH SUCLG1;
RP GTP AND POTASSIUM.
RX PubMed=16481318; DOI=10.1074/jbc.m511785200;
RA Fraser M.E., Hayakawa K., Hume M.S., Ryan D.G., Brownie E.R.;
RT "Interactions of GTP with the ATP-grasp domain of GTP-specific succinyl-CoA
RT synthetase.";
RL J. Biol. Chem. 281:11058-11065(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 40-433 IN COMPLEX WITH SUCLG1.
RX PubMed=26249701; DOI=10.1107/s2053230x15011188;
RA Huang J., Malhi M., Deneke J., Fraser M.E.;
RT "Structure of GTP-specific succinyl-CoA synthetase in complex with CoA.";
RL Acta Crystallogr. F Struct. Biol. Commun. 71:1067-1071(2015).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 40-433 IN COMPLEX WITH SUCLG1 AND
RP SUCCINATE, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27487822; DOI=10.1107/s2059798316010044;
RA Huang J., Fraser M.E.;
RT "Structural basis for the binding of succinate to succinyl-CoA
RT synthetase.";
RL Acta Crystallogr. D 72:912-921(2016).
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:0000255|HAMAP-Rule:MF_03221, ECO:0000269|PubMed:27487822,
CC ECO:0000269|PubMed:8401211}.
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:0000255|HAMAP-
CC Rule:MF_03221, ECO:0000269|PubMed:27487822,
CC ECO:0000269|PubMed:8401211};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03221};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03221};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.76 mM for succinate {ECO:0000269|PubMed:27487822};
CC Vmax=5.99 umol/min/mg enzyme {ECO:0000269|PubMed:27487822};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_03221, ECO:0000305|PubMed:8401211}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta subunit
CC determines specificity for GTP. {ECO:0000255|HAMAP-Rule:MF_03221,
CC ECO:0000269|PubMed:10873456, ECO:0000269|PubMed:16481318,
CC ECO:0000269|PubMed:26249701, ECO:0000269|PubMed:27487822}.
CC -!- INTERACTION:
CC P53590; O19069: SUCLG1; NbExp=2; IntAct=EBI-7317595, EBI-9024832;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03221}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. GTP-specific subunit beta subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03221}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA31120.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L06944; AAA31120.1; ALT_INIT; mRNA.
DR EMBL; Z81187; CAB03559.1; -; mRNA.
DR PIR; A44529; A44529.
DR PDB; 1EUC; X-ray; 2.10 A; B=39-433.
DR PDB; 1EUD; X-ray; 2.10 A; B=39-433.
DR PDB; 2FP4; X-ray; 2.08 A; B=40-433.
DR PDB; 2FPG; X-ray; 2.96 A; B=40-433.
DR PDB; 2FPI; X-ray; 2.70 A; B=40-433.
DR PDB; 2FPP; X-ray; 2.35 A; B=40-433.
DR PDB; 4XX0; X-ray; 2.10 A; B=40-433.
DR PDB; 5CAE; X-ray; 2.20 A; B=40-433.
DR PDB; 6XRU; X-ray; 1.40 A; B=39-433.
DR PDB; 7JFP; X-ray; 2.55 A; B=39-433.
DR PDB; 7JJ0; X-ray; 2.25 A; B/D=39-433.
DR PDB; 7JKR; X-ray; 2.64 A; B=39-433.
DR PDB; 7JMK; X-ray; 2.50 A; B/D=39-433.
DR PDBsum; 1EUC; -.
DR PDBsum; 1EUD; -.
DR PDBsum; 2FP4; -.
DR PDBsum; 2FPG; -.
DR PDBsum; 2FPI; -.
DR PDBsum; 2FPP; -.
DR PDBsum; 4XX0; -.
DR PDBsum; 5CAE; -.
DR PDBsum; 6XRU; -.
DR PDBsum; 7JFP; -.
DR PDBsum; 7JJ0; -.
DR PDBsum; 7JKR; -.
DR PDBsum; 7JMK; -.
DR AlphaFoldDB; P53590; -.
DR SMR; P53590; -.
DR CORUM; P53590; -.
DR IntAct; P53590; 1.
DR MINT; P53590; -.
DR STRING; 9823.ENSSSCP00000012257; -.
DR PaxDb; P53590; -.
DR PeptideAtlas; P53590; -.
DR PRIDE; P53590; -.
DR eggNOG; KOG1447; Eukaryota.
DR InParanoid; P53590; -.
DR BRENDA; 6.2.1.4; 6170.
DR SABIO-RK; P53590; -.
DR UniPathway; UPA00223; UER00999.
DR EvolutionaryTrace; P53590; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0042709; C:succinate-CoA ligase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.261; -; 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 PANTHER; PTHR11815; PTHR11815; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001554; SucCS_beta; 1.
DR SUPFAM; SSF52210; SSF52210; 1.
DR TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; GTP-binding; Ligase;
KW Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT <1..38
FT /note="Mitochondrion"
FT CHAIN 39..433
FT /note="Succinate--CoA ligase [GDP-forming] subunit beta,
FT mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT /id="PRO_0000033358"
FT DOMAIN 47..275
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT BINDING 58
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221,
FT ECO:0000269|PubMed:16481318"
FT BINDING 91..93
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221,
FT ECO:0000269|PubMed:16481318"
FT BINDING 147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221,
FT ECO:0000269|PubMed:16481318"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221,
FT ECO:0000305|PubMed:16481318"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221,
FT ECO:0000305|PubMed:16481318"
FT BINDING 309
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221,
FT ECO:0000269|PubMed:27487822"
FT BINDING 366..368
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221,
FT ECO:0000269|PubMed:27487822"
FT SITE 80
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT SITE 148
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03221"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT MOD_RES 79
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT MOD_RES 133
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT MOD_RES 140
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT MOD_RES 201
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT MOD_RES 228
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96I99"
FT MOD_RES 272
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT MOD_RES 292
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96I99"
FT MOD_RES 339
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT MOD_RES 348
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT MOD_RES 387
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT MOD_RES 424
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2I8"
FT NON_TER 1
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:6XRU"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:6XRU"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6XRU"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:7JMK"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:6XRU"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:6XRU"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:7JMK"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 150..159
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 161..172
FT /evidence="ECO:0007829|PDB:6XRU"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:6XRU"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:6XRU"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:6XRU"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:6XRU"
FT HELIX 216..235
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 238..248
FT /evidence="ECO:0007829|PDB:6XRU"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:1EUC"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:6XRU"
FT HELIX 265..270
FT /evidence="ECO:0007829|PDB:6XRU"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:2FPI"
FT HELIX 285..292
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 301..310
FT /evidence="ECO:0007829|PDB:6XRU"
FT HELIX 311..323
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:6XRU"
FT HELIX 340..352
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 357..368
FT /evidence="ECO:0007829|PDB:6XRU"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:6XRU"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:5CAE"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:6XRU"
FT HELIX 399..408
FT /evidence="ECO:0007829|PDB:6XRU"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:1EUC"
FT HELIX 419..428
FT /evidence="ECO:0007829|PDB:6XRU"
SQ SEQUENCE 433 AA; 46803 MW; AA04B72BC1B80E24 CRC64;
IPAAPVAAQA RKLLRDLAFR PPLLAARSQV VQLTPRRWLN LQEYQSKKLM SDNGVKVQRF
FVADTANEAL EAAKRLNAKE IVLKAQILAG GRGKGVFSSG LKGGVHLTKD PEVVGQLAKQ
MIGYNLATKQ TPKEGVKVNK VMVAEALDIS RETYLAILMD RSCNGPVLVG SPQGGVDIEE
VAASNPELIF KEQIDIIEGI KDSQAQRMAE NLGFLGPLQN QAADQIKKLY NLFLKIDATQ
VEVNPFGETP EGQVVCFDAK INFDDNAEFR QKDIFAMDDK SENEPIENEA AKYDLKYIGL
DGNIACFVNG AGLAMATCDI IFLNGGKPAN FLDLGGGVKE SQVYQAFKLL TADPKVEAIL
VNIFGGIVNC AIIANGITKA CRELELKVPL VVRLEGTNVH EAQNILTNSG LPITSAVDLE
DAAKKAVASV TKK
