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Protein

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

Gene

SUCLG2

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the GTP-dependent ligation of succinate and CoA to form succinyl-CoA.By similarity

Catalytic activityi

GTP + succinate + CoA = GDP + phosphate + succinyl-CoA.

Pathwayi: tricarboxylic acid cycle

This protein is involved in the pathway tricarboxylic acid cycle, which is part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKP53590.
UniPathwayiUPA00223.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial (EC:6.2.1.4)
Alternative name(s):
GTP-specific succinyl-CoA synthetase subunit beta
Succinyl-CoA synthetase beta-G chain
Short name:
SCS-betaG
Gene namesi
Name:SUCLG2
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei‹1 – 38›38MitochondrionAdd
BLAST
Chaini39 – 433395Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrialPRO_0000033358Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741N6-acetyllysineBy similarity
Modified residuei79 – 791N6-succinyllysineBy similarity
Modified residuei133 – 1331N6-acetyllysineBy similarity
Modified residuei140 – 1401N6-acetyllysineBy similarity
Modified residuei162 – 1621PhosphoserineBy similarity
Modified residuei201 – 2011N6-acetyllysineBy similarity
Modified residuei228 – 2281N6-acetyllysineBy similarity
Modified residuei272 – 2721N6-acetyllysineBy similarity
Modified residuei292 – 2921N6-acetyllysineBy similarity
Modified residuei339 – 3391N6-succinyllysineBy similarity
Modified residuei348 – 3481N6-acetyllysineBy similarity
Modified residuei387 – 3871N6-acetyllysineBy similarity
Modified residuei424 – 4241N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP53590.
PeptideAtlasiP53590.
PRIDEiP53590.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.

Protein-protein interaction databases

MINTiMINT-137965.
STRINGi9823.ENSSSCP00000012257.

Structurei

Secondary structure

1
433
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 5210Combined sources
Beta strandi60 – 656Combined sources
Helixi66 – 7611Combined sources
Beta strandi79 – 857Combined sources
Beta strandi88 – 903Combined sources
Helixi92 – 943Combined sources
Beta strandi104 – 1096Combined sources
Helixi111 – 1199Combined sources
Turni120 – 1234Combined sources
Beta strandi124 – 1274Combined sources
Beta strandi141 – 1455Combined sources
Beta strandi150 – 16011Combined sources
Turni161 – 1644Combined sources
Beta strandi165 – 1739Combined sources
Helixi178 – 1847Combined sources
Helixi186 – 1883Combined sources
Beta strandi190 – 1934Combined sources
Turni196 – 1983Combined sources
Helixi202 – 21110Combined sources
Helixi216 – 23520Combined sources
Beta strandi238 – 24811Combined sources
Turni250 – 2523Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi258 – 2636Combined sources
Helixi265 – 2706Combined sources
Helixi272 – 2754Combined sources
Beta strandi281 – 2833Combined sources
Helixi285 – 2928Combined sources
Beta strandi296 – 2994Combined sources
Beta strandi301 – 31010Combined sources
Helixi311 – 32313Combined sources
Beta strandi330 – 3334Combined sources
Helixi340 – 35213Combined sources
Beta strandi358 – 36811Combined sources
Helixi370 – 38415Combined sources
Beta strandi390 – 3967Combined sources
Helixi399 – 40810Combined sources
Beta strandi411 – 4155Combined sources
Helixi419 – 42810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP53590.
SMRiP53590. Positions 39-431.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53590.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 275229ATP-graspAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.Curated

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.
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 AAA31120.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

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
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[»]
ProteinModelPortaliP53590.
SMRiP53590. Positions 39-431.
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.
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.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, characterization, and expression of the beta subunit of pig heart succinyl-CoA synthetase."
    Bailey D.L., Wolodko W.T., Bridger W.A.
    Protein Sci. 2:1255-1262(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-41.
    Tissue: Heart.
  2. "Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
    Winteroe A.K., Fredholm M., Davies W.
    Mamm. Genome 7:509-517(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-82.
    Tissue: Small intestine.

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: July 6, 2016
This is version 129 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.