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Protein

Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial

Gene

SUCLG2

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation2 Publications

Catalytic activityi

GTP + succinate + CoA = GDP + phosphate + succinyl-CoA.UniRule annotation2 Publications

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Kineticsi

  1. KM=0.76 mM for succinate1 Publication
  1. Vmax=5.99 µmol/min/mg enzyme1 Publication

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes succinate from succinyl-CoA (ligase route).UniRule annotation1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (SUCLG1), Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (SUCLG2), Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (SUCLA2)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinate from succinyl-CoA (ligase route), the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei58GTPUniRule annotation1 Publication1
Sitei80Important for substrate specificityUniRule annotation1
Binding sitei147GTP; via amide nitrogen and carbonyl oxygenUniRule annotation1 Publication1
Sitei148Important for substrate specificityUniRule annotation1
Metal bindingi244MagnesiumUniRule annotation1 Publication1
Metal bindingi258MagnesiumUniRule annotation1 Publication1
Binding sitei309Substrate; shared with subunit alphaUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi91 – 93GTPUniRule annotation1 Publication3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKP53590.
UniPathwayiUPA00223; UER00999.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrialUniRule annotation (EC:6.2.1.4UniRule annotation2 Publications)
Alternative name(s):
GTP-specific succinyl-CoA synthetase subunit betaUniRule annotation
Short name:
G-SCSUniRule annotation
Short name:
GTPSCSUniRule annotation
Succinyl-CoA synthetase beta-G chainUniRule annotation
Short name:
SCS-betaGUniRule annotation
Gene namesi
Name:SUCLG2UniRule annotation
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei‹1 – 38MitochondrionAdd BLAST›38
ChainiPRO_000003335839 – 433Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrialUniRule annotationAdd BLAST395

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei74N6-acetyllysineBy similarity1
Modified residuei79N6-succinyllysineBy similarity1
Modified residuei133N6-acetyllysineBy similarity1
Modified residuei140N6-acetyllysineBy similarity1
Modified residuei162PhosphoserineBy similarity1
Modified residuei201N6-acetyllysineBy similarity1
Modified residuei228N6-acetyllysineBy similarity1
Modified residuei272N6-acetyllysineBy similarity1
Modified residuei292N6-acetyllysineBy similarity1
Modified residuei339N6-succinyllysineBy similarity1
Modified residuei348N6-acetyllysineBy similarity1
Modified residuei387N6-acetyllysineBy similarity1
Modified residuei424N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP53590.
PeptideAtlasiP53590.
PRIDEiP53590.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. The beta subunit determines specificity for GTP.UniRule annotation4 Publications

Protein-protein interaction databases

MINTiMINT-137965.
STRINGi9823.ENSSSCP00000012257.

Structurei

Secondary structure

1433
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 52Combined sources10
Beta strandi60 – 65Combined sources6
Helixi66 – 76Combined sources11
Beta strandi79 – 85Combined sources7
Beta strandi88 – 90Combined sources3
Helixi92 – 94Combined sources3
Beta strandi104 – 109Combined sources6
Helixi111 – 119Combined sources9
Turni120 – 123Combined sources4
Beta strandi124 – 127Combined sources4
Beta strandi141 – 145Combined sources5
Beta strandi150 – 160Combined sources11
Turni161 – 164Combined sources4
Beta strandi165 – 173Combined sources9
Helixi178 – 184Combined sources7
Helixi186 – 188Combined sources3
Beta strandi190 – 193Combined sources4
Turni196 – 198Combined sources3
Helixi202 – 211Combined sources10
Helixi216 – 235Combined sources20
Beta strandi238 – 248Combined sources11
Turni250 – 252Combined sources3
Beta strandi254 – 256Combined sources3
Beta strandi258 – 263Combined sources6
Helixi265 – 270Combined sources6
Helixi272 – 275Combined sources4
Beta strandi281 – 283Combined sources3
Helixi285 – 292Combined sources8
Beta strandi296 – 299Combined sources4
Beta strandi301 – 310Combined sources10
Helixi311 – 323Combined sources13
Beta strandi330 – 333Combined sources4
Helixi340 – 352Combined sources13
Beta strandi358 – 368Combined sources11
Helixi370 – 384Combined sources15
Beta strandi390 – 396Combined sources7
Helixi399 – 408Combined sources10
Beta strandi411 – 415Combined sources5
Helixi419 – 428Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EUCX-ray2.10B39-433[»]
1EUDX-ray2.10B39-433[»]
2FP4X-ray2.08B40-433[»]
2FPGX-ray2.96B40-433[»]
2FPIX-ray2.70B40-433[»]
2FPPX-ray2.35B40-433[»]
4XX0X-ray2.10B40-433[»]
5CAEX-ray2.20B40-433[»]
ProteinModelPortaliP53590.
SMRiP53590.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53590.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini47 – 275ATP-graspUniRule annotationAdd BLAST229

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni366 – 368Substrate binding; shared with subunit alphaUniRule annotation1 Publication3

Sequence similaritiesi

Belongs to the succinate/malate CoA ligase beta subunit family. GTP-specific subunit beta subfamily.UniRule annotation
Contains 1 ATP-grasp domain.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2799. Eukaryota.
COG0045. LUCA.
HOGENOMiHOG000007059.
HOVERGENiHBG055555.
InParanoidiP53590.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
HAMAPiMF_00558. Succ_CoA_beta. 1 hit.
MF_03221. Succ_CoA_betaG_euk. 1 hit.
InterProiIPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005811. CoA_ligase.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR005809. Succ_CoA_synthase_bsu.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PANTHERiPTHR11815. PTHR11815. 1 hit.
PfamiPF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF001554. SucCS_beta. 1 hit.
SUPFAMiSSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01016. sucCoAbeta. 1 hit.
PROSITEiPS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53590-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
IPAAPVAAQA RKLLRDLAFR PPLLAARSQV VQLTPRRWLN LQEYQSKKLM
60 70 80 90 100
SDNGVKVQRF FVADTANEAL EAAKRLNAKE IVLKAQILAG GRGKGVFSSG
110 120 130 140 150
LKGGVHLTKD PEVVGQLAKQ MIGYNLATKQ TPKEGVKVNK VMVAEALDIS
160 170 180 190 200
RETYLAILMD RSCNGPVLVG SPQGGVDIEE VAASNPELIF KEQIDIIEGI
210 220 230 240 250
KDSQAQRMAE NLGFLGPLQN QAADQIKKLY NLFLKIDATQ VEVNPFGETP
260 270 280 290 300
EGQVVCFDAK INFDDNAEFR QKDIFAMDDK SENEPIENEA AKYDLKYIGL
310 320 330 340 350
DGNIACFVNG AGLAMATCDI IFLNGGKPAN FLDLGGGVKE SQVYQAFKLL
360 370 380 390 400
TADPKVEAIL VNIFGGIVNC AIIANGITKA CRELELKVPL VVRLEGTNVH
410 420 430
EAQNILTNSG LPITSAVDLE DAAKKAVASV TKK
Length:433
Mass (Da):46,803
Last modified:May 27, 2002 - v2
Checksum:iAA04B72BC1B80E24
GO

Sequence cautioni

The sequence AAA31120 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06944 mRNA. Translation: AAA31120.1. Different initiation.
Z81187 mRNA. Translation: CAB03559.1.
PIRiA44529.
UniGeneiSsc.12108.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06944 mRNA. Translation: AAA31120.1. Different initiation.
Z81187 mRNA. Translation: CAB03559.1.
PIRiA44529.
UniGeneiSsc.12108.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EUCX-ray2.10B39-433[»]
1EUDX-ray2.10B39-433[»]
2FP4X-ray2.08B40-433[»]
2FPGX-ray2.96B40-433[»]
2FPIX-ray2.70B40-433[»]
2FPPX-ray2.35B40-433[»]
4XX0X-ray2.10B40-433[»]
5CAEX-ray2.20B40-433[»]
ProteinModelPortaliP53590.
SMRiP53590.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-137965.
STRINGi9823.ENSSSCP00000012257.

Proteomic databases

PaxDbiP53590.
PeptideAtlasiP53590.
PRIDEiP53590.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2799. Eukaryota.
COG0045. LUCA.
HOGENOMiHOG000007059.
HOVERGENiHBG055555.
InParanoidiP53590.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00999.
SABIO-RKP53590.

Miscellaneous databases

EvolutionaryTraceiP53590.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
HAMAPiMF_00558. Succ_CoA_beta. 1 hit.
MF_03221. Succ_CoA_betaG_euk. 1 hit.
InterProiIPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005811. CoA_ligase.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR005809. Succ_CoA_synthase_bsu.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PANTHERiPTHR11815. PTHR11815. 1 hit.
PfamiPF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF001554. SucCS_beta. 1 hit.
SUPFAMiSSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01016. sucCoAbeta. 1 hit.
PROSITEiPS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSUCB2_PIG
AccessioniPrimary (citable) accession number: P53590
Secondary accession number(s): Q95279
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 27, 2002
Last modified: November 30, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.