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P53590 (SUCB2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:SUCLG2
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length433 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle.

Subunit structure

Heterodimer of an alpha and a beta subunit.

Subcellular location

Mitochondrion.

Sequence similarities

Belongs to the succinate/malate CoA ligase beta subunit family.

Contains 1 ATP-grasp domain.

Sequence caution

The sequence AAA31120.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandGTP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processtricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: InterPro

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

succinate-CoA ligase (GDP-forming) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide‹1 – 38›38Mitochondrion
Chain39 – 433395Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial
PRO_0000033358

Regions

Domain47 – 275229ATP-grasp

Amino acid modifications

Modified residue741N6-acetyllysine By similarity
Modified residue2281N6-acetyllysine By similarity
Modified residue2921N6-acetyllysine By similarity
Modified residue3391N6-acetyllysine By similarity

Experimental info

Non-terminal residue11

Secondary structure

1 ....................................................................... 433
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53590 [UniParc].

Last modified May 27, 2002. Version 2.
Checksum: AA04B72BC1B80E24

FASTA43346,803
        10         20         30         40         50         60 
IPAAPVAAQA RKLLRDLAFR PPLLAARSQV VQLTPRRWLN LQEYQSKKLM SDNGVKVQRF 

        70         80         90        100        110        120 
FVADTANEAL EAAKRLNAKE IVLKAQILAG GRGKGVFSSG LKGGVHLTKD PEVVGQLAKQ 

       130        140        150        160        170        180 
MIGYNLATKQ TPKEGVKVNK VMVAEALDIS RETYLAILMD RSCNGPVLVG SPQGGVDIEE 

       190        200        210        220        230        240 
VAASNPELIF KEQIDIIEGI KDSQAQRMAE NLGFLGPLQN QAADQIKKLY NLFLKIDATQ 

       250        260        270        280        290        300 
VEVNPFGETP EGQVVCFDAK INFDDNAEFR QKDIFAMDDK SENEPIENEA AKYDLKYIGL 

       310        320        330        340        350        360 
DGNIACFVNG AGLAMATCDI IFLNGGKPAN FLDLGGGVKE SQVYQAFKLL TADPKVEAIL 

       370        380        390        400        410        420 
VNIFGGIVNC AIIANGITKA CRELELKVPL VVRLEGTNVH EAQNILTNSG LPITSAVDLE 

       430 
DAAKKAVASV TKK

« Hide

References

« Hide 'large scale' references
[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: 8401211] [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: 8672129] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-82.
Tissue: Small intestine.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L06944 mRNA. Translation: AAA31120.1. Different initiation.
Z81187 mRNA. Translation: CAB03559.1.
PIRA44529.
UniGeneSsc.12108.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EUCX-ray2.10B40-417[»]
1EUDX-ray2.10B40-417[»]
2FP4X-ray2.08B40-433[»]
2FPGX-ray2.96B40-433[»]
2FPIX-ray2.70B40-433[»]
2FPPX-ray2.35B40-433[»]
ProteinModelPortalP53590.
SMRP53590. Positions 39-431.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-137965.
STRINGP53590.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

GeneTreeENSGT00390000010170.
HOVERGENHBG055555.
OrthoDBEOG4RXZ08.

Family and domain databases

InterProIPR013650. 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]
Gene3DG3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit.
G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:3.40.50.261. Succinyl-CoA_synth-like. 1 hit.
PANTHERPTHR11815. CoA_lig_beta. 1 hit.
PfamPF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFPIRSF001554. SucCS_beta. 1 hit.
SUPFAMSSF52210. CoA_ligase. 1 hit.
TIGRFAMsTIGR01016. SucCoAbeta. 1 hit.
PROSITEPS50975. ATP_GRASP. False negative.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSUCB2_PIG
AccessionPrimary (citable) accession number: P53590
Secondary accession number(s): Q95279
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 27, 2002
Last modified: October 19, 2011
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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