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Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (EC 6.2.1.4) (GTP-specific succinyl-CoA synthetase subunit beta) (G-SCS) (GTPSCS) (Succinyl-CoA synthetase beta-G chain) (SCS-betaG) (Fragment)

 SUCB2_PIG               Reviewed;         433 AA.
P53590; Q95279;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
27-MAY-2002, sequence version 2.
05-DEC-2018, entry version 145.
RecName: Full=Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03221};
EC=6.2.1.4 {ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000269|PubMed:27487822, ECO:0000269|PubMed:8401211};
AltName: Full=GTP-specific succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_03221};
Short=G-SCS {ECO:0000255|HAMAP-Rule:MF_03221};
Short=GTPSCS {ECO:0000255|HAMAP-Rule:MF_03221};
AltName: Full=Succinyl-CoA synthetase beta-G chain {ECO:0000255|HAMAP-Rule:MF_03221};
Short=SCS-betaG {ECO:0000255|HAMAP-Rule:MF_03221};
Flags: Precursor; Fragment;
Name=SUCLG2 {ECO:0000255|HAMAP-Rule:MF_03221};
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-41, FUNCTION, AND
CATALYTIC ACTIVITY.
TISSUE=Heart;
PubMed=8401211; DOI=10.1002/pro.5560020808;
Bailey D.L., Wolodko W.T., Bridger W.A.;
"Cloning, characterization, and expression of the beta subunit of pig
heart succinyl-CoA synthetase.";
Protein Sci. 2:1255-1262(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-82.
TISSUE=Small intestine;
PubMed=8672129; DOI=10.1007/s003359900153;
Winteroe A.K., Fredholm M., Davies W.;
"Evaluation and characterization of a porcine small intestine cDNA
library: analysis of 839 clones.";
Mamm. Genome 7:509-517(1996).
[3]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 39-433 IN COMPLEX WITH
SUCLG1.
PubMed=10873456; DOI=10.1006/jmbi.2000.3807;
Fraser M.E., James M.N., Bridger W.A., Wolodko W.T.;
"Phosphorylated and dephosphorylated structures of pig heart, GTP-
specific succinyl-CoA synthetase.";
J. Mol. Biol. 299:1325-1339(2000).
[4]
X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 40-433 IN COMPLEX WITH WITH
SUCLG1; GTP AND POTASSIUM.
PubMed=16481318; DOI=10.1074/jbc.M511785200;
Fraser M.E., Hayakawa K., Hume M.S., Ryan D.G., Brownie E.R.;
"Interactions of GTP with the ATP-grasp domain of GTP-specific
succinyl-CoA synthetase.";
J. Biol. Chem. 281:11058-11065(2006).
[5]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 40-433 IN COMPLEX WITH
SUCLG1.
PubMed=26249701; DOI=10.1107/S2053230X15011188;
Huang J., Malhi M., Deneke J., Fraser M.E.;
"Structure of GTP-specific succinyl-CoA synthetase in complex with
CoA.";
Acta Crystallogr. F Struct. Biol. Commun. 71:1067-1071(2015).
[6]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 40-433 IN COMPLEX WITH
SUCLG1 AND SUCCINATE, FUNCTION, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=27487822; DOI=10.1107/S2059798316010044;
Huang J., Fraser M.E.;
"Structural basis for the binding of succinate to succinyl-CoA
synthetase.";
Acta Crystallogr. D 72:912-921(2016).
-!- FUNCTION: GTP-specific succinyl-CoA synthetase functions in the
citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA
to the synthesis of GTP and thus represents the only step of
substrate-level phosphorylation in the TCA. The beta subunit
provides nucleotide specificity of the enzyme and binds the
substrate succinate, while the binding sites for coenzyme A and
phosphate are found in the alpha subunit. {ECO:0000255|HAMAP-
Rule:MF_03221, ECO:0000269|PubMed:27487822,
ECO:0000269|PubMed:8401211}.
-!- CATALYTIC ACTIVITY:
Reaction=CoA + GTP + succinate = GDP + phosphate + succinyl-CoA;
Xref=Rhea:RHEA:22120, ChEBI:CHEBI:30031, ChEBI:CHEBI:37565,
ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
ChEBI:CHEBI:58189; EC=6.2.1.4; Evidence={ECO:0000255|HAMAP-
Rule:MF_03221, ECO:0000269|PubMed:27487822,
ECO:0000269|PubMed:8401211};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_03221};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
Rule:MF_03221};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.76 mM for succinate {ECO:0000269|PubMed:27487822};
Vmax=5.99 umol/min/mg enzyme {ECO:0000269|PubMed:27487822};
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
succinate from succinyl-CoA (ligase route): step 1/1.
{ECO:0000255|HAMAP-Rule:MF_03221, ECO:0000305|PubMed:8401211}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta
subunit determines specificity for GTP. {ECO:0000255|HAMAP-
Rule:MF_03221, ECO:0000269|PubMed:10873456,
ECO:0000269|PubMed:16481318, ECO:0000269|PubMed:26249701,
ECO:0000269|PubMed:27487822}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-
Rule:MF_03221}.
-!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
subunit family. GTP-specific subunit beta subfamily.
{ECO:0000255|HAMAP-Rule:MF_03221}.
-!- SEQUENCE CAUTION:
Sequence=AAA31120.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; L06944; AAA31120.1; ALT_INIT; mRNA.
EMBL; Z81187; CAB03559.1; -; mRNA.
PIR; A44529; A44529.
UniGene; Ssc.12108; -.
PDB; 1EUC; X-ray; 2.10 A; B=39-433.
PDB; 1EUD; X-ray; 2.10 A; B=39-433.
PDB; 2FP4; X-ray; 2.08 A; B=40-433.
PDB; 2FPG; X-ray; 2.96 A; B=40-433.
PDB; 2FPI; X-ray; 2.70 A; B=40-433.
PDB; 2FPP; X-ray; 2.35 A; B=40-433.
PDB; 4XX0; X-ray; 2.10 A; B=40-433.
PDB; 5CAE; X-ray; 2.20 A; B=40-433.
PDBsum; 1EUC; -.
PDBsum; 1EUD; -.
PDBsum; 2FP4; -.
PDBsum; 2FPG; -.
PDBsum; 2FPI; -.
PDBsum; 2FPP; -.
PDBsum; 4XX0; -.
PDBsum; 5CAE; -.
ProteinModelPortal; P53590; -.
SMR; P53590; -.
CORUM; P53590; -.
MINT; P53590; -.
STRING; 9823.ENSSSCP00000012257; -.
PaxDb; P53590; -.
PeptideAtlas; P53590; -.
PRIDE; P53590; -.
eggNOG; KOG2799; Eukaryota.
eggNOG; COG0045; LUCA.
HOGENOM; HOG000007059; -.
HOVERGEN; HBG055555; -.
InParanoid; P53590; -.
SABIO-RK; P53590; -.
UniPathway; UPA00223; UER00999.
EvolutionaryTrace; P53590; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:UniProtKB-EC.
GO; GO:0006104; P:succinyl-CoA metabolic process; IEA:InterPro.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
Gene3D; 3.30.1490.20; -; 1.
Gene3D; 3.40.50.261; -; 1.
HAMAP; MF_00558; Succ_CoA_beta; 1.
HAMAP; MF_03221; Succ_CoA_betaG_euk; 1.
InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR005811; CoA_ligase.
InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
InterPro; IPR034722; Succ_CoA_betaG_euk.
InterPro; IPR005809; Succ_CoA_synthase_bsu.
InterPro; IPR016102; Succinyl-CoA_synth-like.
PANTHER; PTHR11815; PTHR11815; 1.
Pfam; PF08442; ATP-grasp_2; 1.
Pfam; PF00549; Ligase_CoA; 1.
PIRSF; PIRSF001554; SucCS_beta; 1.
SUPFAM; SSF52210; SSF52210; 1.
TIGRFAMs; TIGR01016; sucCoAbeta; 1.
PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; GTP-binding; Ligase; Magnesium;
Metal-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transit peptide; Tricarboxylic acid cycle.
TRANSIT <1 38 Mitochondrion.
CHAIN 39 433 Succinate--CoA ligase [GDP-forming]
subunit beta, mitochondrial.
{ECO:0000255|HAMAP-Rule:MF_03221}.
/FTId=PRO_0000033358.
DOMAIN 47 275 ATP-grasp. {ECO:0000255|HAMAP-
Rule:MF_03221}.
NP_BIND 91 93 GTP. {ECO:0000255|HAMAP-Rule:MF_03221,
ECO:0000269|PubMed:16481318}.
REGION 366 368 Substrate binding; shared with subunit
alpha. {ECO:0000255|HAMAP-Rule:MF_03221,
ECO:0000269|PubMed:27487822}.
METAL 244 244 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_03221,
ECO:0000305|PubMed:16481318}.
METAL 258 258 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_03221,
ECO:0000305|PubMed:16481318}.
BINDING 58 58 GTP. {ECO:0000255|HAMAP-Rule:MF_03221,
ECO:0000269|PubMed:16481318}.
BINDING 147 147 GTP; via amide nitrogen and carbonyl
oxygen. {ECO:0000255|HAMAP-Rule:MF_03221,
ECO:0000269|PubMed:16481318}.
BINDING 309 309 Substrate; shared with subunit alpha.
{ECO:0000255|HAMAP-Rule:MF_03221,
ECO:0000269|PubMed:27487822}.
SITE 80 80 Important for substrate specificity.
{ECO:0000255|HAMAP-Rule:MF_03221}.
SITE 148 148 Important for substrate specificity.
{ECO:0000255|HAMAP-Rule:MF_03221}.
MOD_RES 74 74 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Z2I8}.
MOD_RES 79 79 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9Z2I8}.
MOD_RES 133 133 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Z2I8}.
MOD_RES 140 140 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Z2I8}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z2I8}.
MOD_RES 201 201 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Z2I8}.
MOD_RES 228 228 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q96I99}.
MOD_RES 272 272 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Z2I8}.
MOD_RES 292 292 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q96I99}.
MOD_RES 339 339 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9Z2I8}.
MOD_RES 348 348 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Z2I8}.
MOD_RES 387 387 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Z2I8}.
MOD_RES 424 424 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Z2I8}.
NON_TER 1 1
HELIX 43 52 {ECO:0000244|PDB:2FP4}.
STRAND 60 65 {ECO:0000244|PDB:2FP4}.
HELIX 66 76 {ECO:0000244|PDB:2FP4}.
STRAND 79 85 {ECO:0000244|PDB:2FP4}.
STRAND 88 90 {ECO:0000244|PDB:2FP4}.
HELIX 92 94 {ECO:0000244|PDB:2FP4}.
STRAND 104 109 {ECO:0000244|PDB:2FP4}.
HELIX 111 119 {ECO:0000244|PDB:2FP4}.
TURN 120 123 {ECO:0000244|PDB:2FP4}.
STRAND 124 127 {ECO:0000244|PDB:2FP4}.
STRAND 141 145 {ECO:0000244|PDB:2FP4}.
STRAND 150 160 {ECO:0000244|PDB:2FP4}.
TURN 161 164 {ECO:0000244|PDB:2FP4}.
STRAND 165 173 {ECO:0000244|PDB:2FP4}.
HELIX 178 184 {ECO:0000244|PDB:2FP4}.
HELIX 186 188 {ECO:0000244|PDB:2FP4}.
STRAND 190 193 {ECO:0000244|PDB:2FP4}.
TURN 196 198 {ECO:0000244|PDB:2FP4}.
HELIX 202 211 {ECO:0000244|PDB:2FP4}.
HELIX 216 235 {ECO:0000244|PDB:2FP4}.
STRAND 238 248 {ECO:0000244|PDB:2FP4}.
TURN 250 252 {ECO:0000244|PDB:1EUC}.
STRAND 254 256 {ECO:0000244|PDB:2FP4}.
STRAND 258 263 {ECO:0000244|PDB:2FP4}.
HELIX 265 270 {ECO:0000244|PDB:2FP4}.
HELIX 272 275 {ECO:0000244|PDB:2FP4}.
STRAND 281 283 {ECO:0000244|PDB:2FPI}.
HELIX 285 292 {ECO:0000244|PDB:2FP4}.
STRAND 296 299 {ECO:0000244|PDB:2FP4}.
STRAND 301 310 {ECO:0000244|PDB:2FP4}.
HELIX 311 323 {ECO:0000244|PDB:2FP4}.
STRAND 330 333 {ECO:0000244|PDB:2FP4}.
HELIX 340 352 {ECO:0000244|PDB:2FP4}.
STRAND 358 368 {ECO:0000244|PDB:2FP4}.
HELIX 370 384 {ECO:0000244|PDB:2FP4}.
STRAND 390 396 {ECO:0000244|PDB:2FP4}.
HELIX 399 408 {ECO:0000244|PDB:2FP4}.
STRAND 411 415 {ECO:0000244|PDB:1EUC}.
HELIX 419 428 {ECO:0000244|PDB:2FP4}.
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


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