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Protein

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

Gene

OXCT1

Organism
Homo sapiens (Human)
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 annotation

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 2, mitochondrial (OXCT2), Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial (OXCT1), Succinyl-CoA:3-ketoacid-coenzyme A transferase, Succinyl-CoA:3-ketoacid-coenzyme A transferase (OXCT1), Succinyl-CoA:3-ketoacid-coenzyme A transferase (OXCT)
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)DescriptionActionsGraphical viewLength
Active sitei3445-glutamyl coenzyme A thioester intermediatePROSITE-ProRule annotation1

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

BioCyciMetaCyc:HS01447-MONOMER.
ZFISH:HS01447-MONOMER.
BRENDAi2.8.3.5. 2681.
ReactomeiR-HSA-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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:8527. OXCT1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Succinyl-CoA:3-oxoacid CoA transferase deficiency (SCOTD)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of ketone body metabolism, characterized by episodic ketoacidosis. Patients are usually asymptomatic between episodes.
See also OMIM:245050
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_000696133V → E in SCOTD. 1 PublicationCorresponds to variant rs267606930dbSNPEnsembl.1
Natural variantiVAR_065564215A → V in SCOTD; partial loss of activity. 1 PublicationCorresponds to variant rs201752548dbSNPEnsembl.1
Natural variantiVAR_010337219G → E in SCOTD. 1 PublicationCorresponds to variant rs121909302dbSNPEnsembl.1
Natural variantiVAR_010338221V → M in SCOTD. 1 PublicationCorresponds to variant rs121909303dbSNPEnsembl.1
Natural variantiVAR_065565226S → N in SCOTD; loss of activity. 1 PublicationCorresponds to variant rs368841359dbSNPEnsembl.1
Natural variantiVAR_010339324G → E in SCOTD. 1 PublicationCorresponds to variant rs121909301dbSNPEnsembl.1
Natural variantiVAR_065566327L → P in SCOTD; partial loss of activity. 1 Publication1
Natural variantiVAR_065567404V → F in SCOTD; loss of activity. 1 Publication1
Natural variantiVAR_065568405S → P in SCOTD; loss of activity. 1 Publication1
Natural variantiVAR_000697456C → F in SCOTD. 1 PublicationCorresponds to variant rs121909300dbSNPEnsembl.1
Natural variantiVAR_065569468R → C in SCOTD; partial loss of activity; the mutant retains half of the activity of the wild-type at 30 degrees. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi5019.
MalaCardsiOXCT1.
MIMi245050. phenotype.
OpenTargetsiENSG00000083720.
Orphaneti832. Succinyl-CoA:3-ketoacid CoA transferase deficiency.
PharmGKBiPA32855.

Chemistry databases

DrugBankiDB00139. Succinic acid.

Polymorphism and mutation databases

BioMutaiOXCT1.
DMDMi2492998.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 39Mitochondrion1 PublicationAdd BLAST39
ChainiPRO_000000241340 – 520Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrialAdd BLAST481

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei170PhosphoserineCombined sources1
Modified residuei185N6-succinyllysineBy similarity1
Modified residuei418N6-succinyllysineBy similarity1
Modified residuei421N6-succinyllysineBy similarity1
Modified residuei455N6-succinyllysineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP55809.
MaxQBiP55809.
PaxDbiP55809.
PeptideAtlasiP55809.
PRIDEiP55809.

2D gel databases

UCD-2DPAGEP55809.

PTM databases

iPTMnetiP55809.
PhosphoSitePlusiP55809.

Expressioni

Tissue specificityi

Abundant in heart, followed in order by kidney, brain, and muscle, whereas in liver it is undetectable; also detectable in leukocytes and fibroblasts.

Gene expression databases

BgeeiENSG00000083720.
CleanExiHS_OXCT1.
ExpressionAtlasiP55809. baseline and differential.
GenevisibleiP55809. HS.

Organism-specific databases

HPAiHPA012047.
HPA061425.

Interactioni

Subunit structurei

Homodimer.

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi111059. 64 interactors.
IntActiP55809. 5 interactors.
STRINGi9606.ENSP00000196371.

Structurei

Secondary structure

1520
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi41 – 44Combined sources4
Helixi46 – 50Combined sources5
Beta strandi58 – 61Combined sources4
Helixi71 – 80Combined sources10
Beta strandi84 – 88Combined sources5
Helixi100 – 104Combined sources5
Beta strandi108 – 114Combined sources7
Helixi120 – 127Combined sources8
Beta strandi130 – 135Combined sources6
Helixi138 – 150Combined sources13
Beta strandi154 – 158Combined sources5
Turni159 – 162Combined sources4
Helixi164 – 167Combined sources4
Beta strandi171 – 174Combined sources4
Beta strandi178 – 183Combined sources6
Beta strandi189 – 192Combined sources4
Beta strandi195 – 201Combined sources7
Beta strandi205 – 211Combined sources7
Beta strandi213 – 216Combined sources4
Helixi225 – 227Combined sources3
Helixi231 – 234Combined sources4
Beta strandi237 – 249Combined sources13
Helixi256 – 258Combined sources3
Helixi263 – 265Combined sources3
Beta strandi268 – 271Combined sources4
Helixi300 – 309Combined sources10
Helixi310 – 312Combined sources3
Beta strandi318 – 321Combined sources4
Helixi325 – 329Combined sources5
Helixi330 – 332Combined sources3
Beta strandi340 – 343Combined sources4
Turni344 – 346Combined sources3
Beta strandi347 – 350Combined sources4
Helixi356 – 358Combined sources3
Beta strandi368 – 370Combined sources3
Beta strandi373 – 379Combined sources7
Helixi382 – 390Combined sources9
Beta strandi395 – 399Combined sources5
Beta strandi402 – 405Combined sources4
Beta strandi413 – 415Combined sources3
Turni416 – 418Combined sources3
Helixi426 – 429Combined sources4
Beta strandi435 – 440Combined sources6
Helixi446 – 448Combined sources3
Beta strandi450 – 455Combined sources6
Beta strandi461 – 464Combined sources4
Beta strandi468 – 470Combined sources3
Beta strandi472 – 479Combined sources8
Turni480 – 482Combined sources3
Beta strandi483 – 489Combined sources7
Helixi495 – 499Combined sources5
Beta strandi502 – 504Combined sources3
Beta strandi507 – 514Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DLXX-ray2.20A/B/C/D40-520[»]
ProteinModelPortaliP55809.
SMRiP55809.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55809.

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.
GeneTreeiENSGT00390000009130.
HOGENOMiHOG000221245.
HOVERGENiHBG002310.
InParanoidiP55809.
KOiK01027.
OMAiNIQFRHA.
OrthoDBiEOG091G0D3X.
PhylomeDBiP55809.
TreeFamiTF313991.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P55809-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAALKLLSSG LRLCASARGS GATWYKGCVC SFSTSAHRHT KFYTDPVEAV
60 70 80 90 100
KDIPDGATVL VGGFGLCGIP ENLIDALLKT GVKGLTAVSN NAGVDNFGLG
110 120 130 140 150
LLLRSKQIKR MVSSYVGENA EFERQYLSGE LEVELTPQGT LAERIRAGGA
160 170 180 190 200
GVPAFYTPTG YGTLVQEGGS PIKYNKDGSV AIASKPREVR EFNGQHFILE
210 220 230 240 250
EAITGDFALV KAWKADRAGN VIFRKSARNF NLPMCKAAET TVVEVEEIVD
260 270 280 290 300
IGAFAPEDIH IPQIYVHRLI KGEKYEKRIE RLSIRKEGDG EAKSAKPGDD
310 320 330 340 350
VRERIIKRAA LEFEDGMYAN LGIGIPLLAS NFISPNITVH LQSENGVLGL
360 370 380 390 400
GPYPRQHEAD ADLINAGKET VTILPGASFF SSDESFAMIR GGHVDLTMLG
410 420 430 440 450
AMQVSKYGDL ANWMIPGKMV KGMGGAMDLV SSAKTKVVVT MEHSAKGNAH
460 470 480 490 500
KIMEKCTLPL TGKQCVNRII TEKAVFDVDK KKGLTLIELW EGLTVDDVQK
510 520
STGCDFAVSP KLMPMQQIAN
Length:520
Mass (Da):56,158
Last modified:November 1, 1997 - v1
Checksum:i54DA790FB8EDA546
GO
Isoform 2 (identifier: P55809-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-397: Missing.

Note: No experimental confirmation available.
Show »
Length:123
Mass (Da):13,358
Checksum:i5B36DC7CF0E0B843
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti95D → G in BAG35249 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00069558T → M.2 PublicationsCorresponds to variant rs75134564dbSNPEnsembl.1
Natural variantiVAR_000696133V → E in SCOTD. 1 PublicationCorresponds to variant rs267606930dbSNPEnsembl.1
Natural variantiVAR_065564215A → V in SCOTD; partial loss of activity. 1 PublicationCorresponds to variant rs201752548dbSNPEnsembl.1
Natural variantiVAR_010337219G → E in SCOTD. 1 PublicationCorresponds to variant rs121909302dbSNPEnsembl.1
Natural variantiVAR_010338221V → M in SCOTD. 1 PublicationCorresponds to variant rs121909303dbSNPEnsembl.1
Natural variantiVAR_065565226S → N in SCOTD; loss of activity. 1 PublicationCorresponds to variant rs368841359dbSNPEnsembl.1
Natural variantiVAR_010339324G → E in SCOTD. 1 PublicationCorresponds to variant rs121909301dbSNPEnsembl.1
Natural variantiVAR_065566327L → P in SCOTD; partial loss of activity. 1 Publication1
Natural variantiVAR_065567404V → F in SCOTD; loss of activity. 1 Publication1
Natural variantiVAR_065568405S → P in SCOTD; loss of activity. 1 Publication1
Natural variantiVAR_000697456C → F in SCOTD. 1 PublicationCorresponds to variant rs121909300dbSNPEnsembl.1
Natural variantiVAR_065569468R → C in SCOTD; partial loss of activity; the mutant retains half of the activity of the wild-type at 30 degrees. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0563101 – 397Missing in isoform 2. 1 PublicationAdd BLAST397

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62961 mRNA. Translation: AAB07366.1.
AB029576 Genomic DNA. Translation: BAB13733.1.
AK298352 mRNA. Translation: BAH12764.1.
AK312327 mRNA. Translation: BAG35249.1.
AK315902 mRNA. Translation: BAH14273.1.
AC008817 Genomic DNA. No translation available.
AC034222 Genomic DNA. No translation available.
AC114946 Genomic DNA. No translation available.
BC009001 mRNA. Translation: AAH09001.1.
CCDSiCCDS3937.1. [P55809-1]
RefSeqiNP_000427.1. NM_000436.3. [P55809-1]
UniGeneiHs.278277.

Genome annotation databases

EnsembliENST00000196371; ENSP00000196371; ENSG00000083720. [P55809-1]
ENST00000510634; ENSP00000423144; ENSG00000083720. [P55809-2]
ENST00000512084; ENSP00000421143; ENSG00000083720. [P55809-2]
GeneIDi5019.
KEGGihsa:5019.
UCSCiuc003jmn.4. human. [P55809-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62961 mRNA. Translation: AAB07366.1.
AB029576 Genomic DNA. Translation: BAB13733.1.
AK298352 mRNA. Translation: BAH12764.1.
AK312327 mRNA. Translation: BAG35249.1.
AK315902 mRNA. Translation: BAH14273.1.
AC008817 Genomic DNA. No translation available.
AC034222 Genomic DNA. No translation available.
AC114946 Genomic DNA. No translation available.
BC009001 mRNA. Translation: AAH09001.1.
CCDSiCCDS3937.1. [P55809-1]
RefSeqiNP_000427.1. NM_000436.3. [P55809-1]
UniGeneiHs.278277.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DLXX-ray2.20A/B/C/D40-520[»]
ProteinModelPortaliP55809.
SMRiP55809.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111059. 64 interactors.
IntActiP55809. 5 interactors.
STRINGi9606.ENSP00000196371.

Chemistry databases

DrugBankiDB00139. Succinic acid.

PTM databases

iPTMnetiP55809.
PhosphoSitePlusiP55809.

Polymorphism and mutation databases

BioMutaiOXCT1.
DMDMi2492998.

2D gel databases

UCD-2DPAGEP55809.

Proteomic databases

EPDiP55809.
MaxQBiP55809.
PaxDbiP55809.
PeptideAtlasiP55809.
PRIDEiP55809.

Protocols and materials databases

DNASUi5019.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000196371; ENSP00000196371; ENSG00000083720. [P55809-1]
ENST00000510634; ENSP00000423144; ENSG00000083720. [P55809-2]
ENST00000512084; ENSP00000421143; ENSG00000083720. [P55809-2]
GeneIDi5019.
KEGGihsa:5019.
UCSCiuc003jmn.4. human. [P55809-1]

Organism-specific databases

CTDi5019.
DisGeNETi5019.
GeneCardsiOXCT1.
HGNCiHGNC:8527. OXCT1.
HPAiHPA012047.
HPA061425.
MalaCardsiOXCT1.
MIMi245050. phenotype.
601424. gene.
neXtProtiNX_P55809.
OpenTargetsiENSG00000083720.
Orphaneti832. Succinyl-CoA:3-ketoacid CoA transferase deficiency.
PharmGKBiPA32855.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3822. Eukaryota.
COG1788. LUCA.
COG2057. LUCA.
GeneTreeiENSGT00390000009130.
HOGENOMiHOG000221245.
HOVERGENiHBG002310.
InParanoidiP55809.
KOiK01027.
OMAiNIQFRHA.
OrthoDBiEOG091G0D3X.
PhylomeDBiP55809.
TreeFamiTF313991.

Enzyme and pathway databases

UniPathwayiUPA00929; UER00894.
BioCyciMetaCyc:HS01447-MONOMER.
ZFISH:HS01447-MONOMER.
BRENDAi2.8.3.5. 2681.
ReactomeiR-HSA-77108. Utilization of Ketone Bodies.

Miscellaneous databases

EvolutionaryTraceiP55809.
GeneWikiiOXCT1.
GenomeRNAii5019.
PROiP55809.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000083720.
CleanExiHS_OXCT1.
ExpressionAtlasiP55809. baseline and differential.
GenevisibleiP55809. HS.

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...

Entry informationi

Entry nameiSCOT1_HUMAN
AccessioniPrimary (citable) accession number: P55809
Secondary accession number(s): B2R5V2, B7Z528
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.