Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q5XIJ9

Entry ID Method Resolution Chain Position Source
AF-Q5XIJ9-F1 Predicted AlphaFoldDB

No variants for Q5XIJ9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5XIJ9

No associated diseases with Q5XIJ9

4 regional properties for Q5XIJ9

Type Name Position InterPro Accession
binding_site Coenzyme A transferase binding site 55 - 70 IPR004163
active_site Coenzyme A transferase active site 339 - 347 IPR004164
domain 3-oxoacid CoA-transferase, subunit B 300 - 505 IPR012791
domain 3-oxoacid CoA-transferase, subunit A 43 - 168 IPR012792

Functions

Description
EC Number 2.8.3.5 CoA-transferases
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
motile cilium A cilium which may have a variable arrangement of axonemal microtubules and also contains molecular motors. It may beat with a whip-like pattern that promotes cell motility or transport of fluids and other cells across a cell surface, such as on epithelial cells that line the lumenal ducts of various tissues; or they may display a distinct twirling motion that directs fluid flow asymmetrically across the cellular surface to affect asymmetric body plan organization. Motile cilia can be found in single as well as multiple copies per cell.

2 GO annotations of molecular function

Name Definition
3-oxoacid CoA-transferase activity Catalysis of the reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxo-acyl-CoA.
CoA-transferase activity Catalysis of the transfer of a coenzyme A (CoA) group from one compound (donor) to another (acceptor).

2 GO annotations of biological process

Name Definition
cellular ketone body metabolic process The chemical reactions and pathways involving ketone bodies, any one of the three substances: acetoacetate, D-3-hydroxybutyrate (beta-hydroxybutyrate) or acetone, as carried out by individual cells. Although 3-hydroxybutyrate is not a ketone, it is classed as a ketone body because it exists in an equilibrium with acetoacetate. Ketone bodies may accumulate in excessive amounts in the body in starvation, diabetes mellitus or in other defects of carbohydrate metabolism.
ketone body catabolic process The chemical reactions and pathways resulting in the breakdown of ketone bodies, any one of the three substances: acetoacetate, D-3-hydroxybutyrate (beta-hydroxybutyrate) or acetone. Ketone bodies can be used as an energy source as an alternative to glucose. Utilization of ketone bodies in peripheral tissues involves conversion of acetoacetate to acetoacetyl-CoA, which is then converted to two molecules of acetyl-CoA.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9BYC2 OXCT2 Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial Homo sapiens (Human) PR
10 20 30 40 50 60
MAALRLLAWA FSRRVSAHRP QPTLPHHLIR HYPTTRCGKV KFYTDPVKAV EGIKDGASVM
70 80 90 100 110 120
LGGFGLCGIP ENLIGALKTK GVKDLKIISS NVGVDDFGLG ILLASKQVRR VVCSYLGENK
130 140 150 160 170 180
LCEQLYLAGK LELEMTPQGT LAERIRAGGT GVPAFYTPTG YGTQVQEGGV PIRYSPEGHL
190 200 210 220 230 240
ITLSQPREVR EFEGQHHLLE RAIRADFALI KGWKADRSGN VIFRGSARNF NVPMCKAADI
250 260 270 280 290 300
SVVEVEEIVD VGTFAPEDIH IPNIYVKRVI KGPRFEKRIE RLTTRDSPPA PGSKDQDPKR
310 320 330 340 350 360
TRIIKRAALE FKDGMYANLG IGIPVLASNY ISPKMTVYLH SENGILGLGP FPLKKEVDPD
370 380 390 400 410 420
IINAGKQTVT VIPGGCFFAS DDSFAMIRGG HIQLTMLGAM QVSKYGDLAN WMVPGKKVKG
430 440 450 460 470 480
MGGAMDLVSS KKTKVVVTME HCTKTKQPKI LEKCTMPLTG KSCVDLIITE KAVFEVDRSK
490 500 510
GLKLVELWEG SSLDEVKATT GCSFKVCPNL KPMQQIKSDA