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Protein

Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial

Gene

OXCT1

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

Functioni

Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate.

Catalytic activityi

Succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA.PROSITE-ProRule annotation2 Publications

Pathwayi: succinyl-CoA degradation

This protein is involved in step 1 of the subpathway that synthesizes acetoacetyl-CoA from succinyl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Succinyl-CoA:3-ketoacid-coenzyme A transferase, Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial (OXCT1)
This subpathway is part of the pathway succinyl-CoA degradation, which is itself part of Ketone metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetoacetyl-CoA from succinyl-CoA, the pathway succinyl-CoA degradation and in Ketone metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei344 – 34415-glutamyl coenzyme A thioester intermediatePROSITE-ProRule annotation1 Publication

GO - Molecular functioni

  • 3-oxoacid CoA-transferase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.8.3.5. 6170.
ReactomeiR-SSC-77108. Utilization of Ketone Bodies.
UniPathwayiUPA00929; UER00894.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial (EC:2.8.3.5)
Alternative name(s):
3-oxoacid CoA-transferase 1
Somatic-type succinyl-CoA:3-oxoacid CoA-transferase
Short name:
SCOT-s
Gene namesi
Name:OXCT1
Synonyms:OXCT, SCOT
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671C → A: Decreases KM for acetoacetyl-CoA 3-fold. No effect on KM for acetoacetate, succinyl-CoA and succinate. 1 Publication
Mutagenesisi67 – 671C → S: Decreases KM for acetoacetate and acetoacetyl-CoA 2-fold. Increases KM for succinate 2-fold. Decreases KM for succinyl-CoA nearly 4-fold. Strongly reduces catalytic activity. 1 Publication
Mutagenesisi235 – 2351C → S: Similar specific activity to wild-type. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3939Mitochondrion1 PublicationAdd
BLAST
Chaini40 – 520481Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrialPRO_0000002415Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei170 – 1701PhosphoserineBy similarity
Modified residuei185 – 1851N6-succinyllysineBy similarity
Modified residuei418 – 4181N6-succinyllysineBy similarity
Modified residuei421 – 4211N6-succinyllysineBy similarity
Modified residuei455 – 4551N6-succinyllysineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ29551.
PRIDEiQ29551.

Expressioni

Gene expression databases

GenevisibleiQ29551. SS.

Interactioni

Subunit structurei

Homodimer.6 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000017870.

Structurei

Secondary structure

1
520
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 444Combined sources
Helixi46 – 505Combined sources
Beta strandi58 – 614Combined sources
Helixi71 – 8010Combined sources
Beta strandi84 – 885Combined sources
Helixi100 – 1045Combined sources
Beta strandi108 – 1147Combined sources
Helixi120 – 1278Combined sources
Beta strandi130 – 1356Combined sources
Helixi138 – 14912Combined sources
Beta strandi154 – 1585Combined sources
Turni159 – 1624Combined sources
Helixi164 – 1674Combined sources
Beta strandi171 – 1744Combined sources
Beta strandi178 – 1836Combined sources
Beta strandi189 – 1924Combined sources
Beta strandi195 – 2017Combined sources
Beta strandi205 – 21612Combined sources
Helixi225 – 2273Combined sources
Helixi231 – 2344Combined sources
Beta strandi237 – 24913Combined sources
Helixi256 – 2583Combined sources
Helixi263 – 2653Combined sources
Beta strandi268 – 2714Combined sources
Helixi302 – 3098Combined sources
Helixi310 – 3123Combined sources
Beta strandi317 – 3215Combined sources
Helixi325 – 3295Combined sources
Helixi330 – 3323Combined sources
Beta strandi339 – 3435Combined sources
Turni344 – 3463Combined sources
Beta strandi347 – 3504Combined sources
Helixi356 – 3583Combined sources
Beta strandi368 – 3703Combined sources
Beta strandi373 – 3797Combined sources
Helixi382 – 3909Combined sources
Beta strandi395 – 3995Combined sources
Beta strandi402 – 4054Combined sources
Beta strandi413 – 4153Combined sources
Turni416 – 4183Combined sources
Helixi426 – 4294Combined sources
Beta strandi435 – 4406Combined sources
Beta strandi443 – 4453Combined sources
Helixi446 – 4483Combined sources
Beta strandi450 – 4556Combined sources
Beta strandi461 – 4644Combined sources
Beta strandi468 – 4703Combined sources
Beta strandi472 – 4798Combined sources
Turni480 – 4823Combined sources
Beta strandi483 – 4897Combined sources
Helixi495 – 5006Combined sources
Beta strandi502 – 5043Combined sources
Beta strandi507 – 5148Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M3EX-ray2.50A/B/C/D40-520[»]
1O9LX-ray2.40A/B/C/D40-520[»]
1OOYX-ray1.70A/B40-520[»]
1OOZX-ray2.10A/B40-520[»]
1OPEX-ray2.50A/B40-520[»]
2NRBX-ray2.00A/B/C/D40-520[»]
2NRCX-ray2.05A/B/C/D40-520[»]
3K6MX-ray1.50A/B/C/D40-520[»]
3OXOX-ray2.30A/B/C/D/E/F/G/H40-517[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ29551.

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-oxoacid CoA-transferase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3822. Eukaryota.
COG1788. LUCA.
COG2057. LUCA.
HOVERGENiHBG002310.
InParanoidiQ29551.
KOiK01027.

Family and domain databases

InterProiIPR012792. 3-oxoacid_CoA-transf_A.
IPR012791. 3-oxoacid_CoA-transf_B.
IPR014388. 3-oxoacid_CoA-transferase.
IPR004165. CoA_trans_fam_I.
IPR004164. CoA_transf_AS.
IPR004163. CoA_transf_BS.
[Graphical view]
PANTHERiPTHR13707. PTHR13707. 1 hit.
PfamiPF01144. CoA_trans. 2 hits.
[Graphical view]
PIRSFiPIRSF000858. SCOT-t. 1 hit.
SMARTiSM00882. CoA_trans. 2 hits.
[Graphical view]
TIGRFAMsiTIGR02429. pcaI_scoA_fam. 1 hit.
TIGR02428. pcaJ_scoB_fam. 1 hit.
PROSITEiPS01273. COA_TRANSF_1. 1 hit.
PS01274. COA_TRANSF_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q29551-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALTLLSSR LRLCASAYRS GGAWSQGCAG YFSTSTRRHT KFYTDAVEAV
60 70 80 90 100
KDIPNGATVL VGGFGLCGIP ENLIGALLKT GVKELTAVSN NAGVDNFGLG
110 120 130 140 150
LLLQSKQIKR MISSYVGENA EFERQYLAGE LEVELTPQGT LAERIRAGGA
160 170 180 190 200
GVPAFYTSTG YGTLVQEGGS PIKYNKDGSI AIASKPREVR EFNGQHFILE
210 220 230 240 250
EAIRGDFALV KAWKADQAGN VTFRKSARNF NLPMCKAAET TVVEVEEIVD
260 270 280 290 300
IGSFAPEDIH IPKIYVHRLV KGEKYEKRIE RLSVRKEEDV KTRSGKLGDN
310 320 330 340 350
VRERIIKRAA LEFEDGMYAN LGIGIPLLAS NFISPNMTVH LQSENGILGL
360 370 380 390 400
GPYPLQNEVD ADLINAGKET VTVLPGASYF SSDESFAMIR GGHVNLTMLG
410 420 430 440 450
AMQVSKYGDL ANWMIPGKLV KGMGGAMDLV SSAKTKVVVT MEHSAKGNAH
460 470 480 490 500
KIMEKCTLPL TGKQCVNRII TEKAVFDVDS KKGLTLIELW EGLTVDDIKK
510 520
STGCDFAVSP KLIPMQQVTT
Length:520
Mass (Da):56,338
Last modified:July 11, 2012 - v2
Checksum:i3DCFE430FE78C222
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti480 – 4801S → R in AAA31019 (PubMed:1730685).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80534 mRNA. Translation: AAA31019.1.
CU993811 Genomic DNA. No translation available.
FP017290 Genomic DNA. No translation available.
PIRiA41771.
RefSeqiNP_999103.1. NM_213938.1.
UniGeneiSsc.27309.

Genome annotation databases

GeneIDi396978.
KEGGissc:396978.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80534 mRNA. Translation: AAA31019.1.
CU993811 Genomic DNA. No translation available.
FP017290 Genomic DNA. No translation available.
PIRiA41771.
RefSeqiNP_999103.1. NM_213938.1.
UniGeneiSsc.27309.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M3EX-ray2.50A/B/C/D40-520[»]
1O9LX-ray2.40A/B/C/D40-520[»]
1OOYX-ray1.70A/B40-520[»]
1OOZX-ray2.10A/B40-520[»]
1OPEX-ray2.50A/B40-520[»]
2NRBX-ray2.00A/B/C/D40-520[»]
2NRCX-ray2.05A/B/C/D40-520[»]
3K6MX-ray1.50A/B/C/D40-520[»]
3OXOX-ray2.30A/B/C/D/E/F/G/H40-517[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000017870.

Proteomic databases

PaxDbiQ29551.
PRIDEiQ29551.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396978.
KEGGissc:396978.

Organism-specific databases

CTDi5019.

Phylogenomic databases

eggNOGiKOG3822. Eukaryota.
COG1788. LUCA.
COG2057. LUCA.
HOVERGENiHBG002310.
InParanoidiQ29551.
KOiK01027.

Enzyme and pathway databases

UniPathwayiUPA00929; UER00894.
BRENDAi2.8.3.5. 6170.
ReactomeiR-SSC-77108. Utilization of Ketone Bodies.

Miscellaneous databases

EvolutionaryTraceiQ29551.

Gene expression databases

GenevisibleiQ29551. SS.

Family and domain databases

InterProiIPR012792. 3-oxoacid_CoA-transf_A.
IPR012791. 3-oxoacid_CoA-transf_B.
IPR014388. 3-oxoacid_CoA-transferase.
IPR004165. CoA_trans_fam_I.
IPR004164. CoA_transf_AS.
IPR004163. CoA_transf_BS.
[Graphical view]
PANTHERiPTHR13707. PTHR13707. 1 hit.
PfamiPF01144. CoA_trans. 2 hits.
[Graphical view]
PIRSFiPIRSF000858. SCOT-t. 1 hit.
SMARTiSM00882. CoA_trans. 2 hits.
[Graphical view]
TIGRFAMsiTIGR02429. pcaI_scoA_fam. 1 hit.
TIGR02428. pcaJ_scoB_fam. 1 hit.
PROSITEiPS01273. COA_TRANSF_1. 1 hit.
PS01274. COA_TRANSF_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a cDNA clone encoding pig heart mitochondrial CoA transferase."
    Lin T., Bridger W.A.
    J. Biol. Chem. 267:975-978(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 40-70 AND 296-305.
    Tissue: Heart.
  2. Swine Genome Sequencing Consortium.
    Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Identification of glutamate 344 as the catalytic residue in the active site of pig heart CoA transferase."
    Rochet J.C., Bridger W.A.
    Protein Sci. 3:975-981(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE.
  4. "Structure of the mammalian CoA transferase from pig heart."
    Bateman K.S., Brownie E.R., Wolodko W.T., Fraser M.E.
    Biochemistry 41:14455-14462(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-520, SUBUNIT.
    Tissue: Heart.
  5. "Succinate:Coenzyme-A transferase deficiency: A structural view of pathogenic mutations."
    Mitchell E.P., Lloyd A.J., Lewis G., Shoolingin-Jordan P.
    Submitted (DEC-2002) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 40-520, SUBUNIT.
    Tissue: Heart.
  6. "Structure of the CoA transferase from pig heart to 1.7 A resolution."
    Coros A.M., Swenson L., Wolodko W.T., Fraser M.E.
    Acta Crystallogr. D 60:1717-1725(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 40-520, SUBUNIT.
    Tissue: Heart.
  7. "Identification of the cysteine residue exposed by the conformational change in pig heart succinyl-CoA:3-ketoacid coenzyme A transferase on binding coenzyme A."
    Tammam S.D., Rochet J.C., Fraser M.E.
    Biochemistry 46:10852-10863(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 40-520 OF MUTANTS ALA/SER-67, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF CYS-67 AND CYS-235, REACTION MECHANISM.
    Tissue: Heart.
  8. "The high-resolution structure of pig heart succinyl-CoA:3-oxoacid coenzyme A transferase."
    Coker S.F., Lloyd A.J., Mitchell E., Lewis G.R., Coker A.R., Shoolingin-Jordan P.M.
    Acta Crystallogr. D 66:797-805(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 40-520, SUBUNIT.
    Tissue: Heart.
  9. "Catalytic role of the conformational change in succinyl-CoA:3-oxoacid CoA transferase on binding CoA."
    Fraser M.E., Hayakawa K., Brown W.D.
    Biochemistry 49:10319-10328(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 40-517 IN COMPLEX WITH REACTION INTERMEDIATE, CATALYTIC ACTIVITY, SUBUNIT.
    Tissue: Heart.

Entry informationi

Entry nameiSCOT1_PIG
AccessioniPrimary (citable) accession number: Q29551
Secondary accession number(s): F1SMH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 11, 2012
Last modified: February 17, 2016
This is version 106 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.