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 Q8K0L3

Entry ID Method Resolution Chain Position Source
AF-Q8K0L3-F1 Predicted AlphaFoldDB

37 variants for Q8K0L3

Variant ID(s) Position Change Description Diseaes Association Provenance
rs228867113 21 R>C No EVA
rs3388941652 27 I>N No EVA
rs3388939240 34 Q>E No EVA
rs243000849 57 V>I No EVA
rs231762316 84 R>Q No EVA
rs3388899046 137 T>S No EVA
rs3388939694 167 V>L No EVA
rs3388945798 185 E>G No EVA
rs3388915023 189 E>D No EVA
rs32561385 213 R>Q No EVA
rs3388944974 233 H>L No EVA
rs3398553324 248 S>R No EVA
rs227696573 268 M>L No EVA
rs3388899061 276 E>D No EVA
rs213845667 288 L>V No EVA
rs3398481993 289 L>* No EVA
rs32557893 303 S>R No EVA
rs257616574 308 T>S No EVA
rs227884249 308 T>S No EVA
rs219602722 315 I>V No EVA
rs221980725 361 I>F No EVA
rs221723292 370 I>T No EVA
rs3388945121 371 C>Y No EVA
rs32560048 389 A>P No EVA
rs32562165 418 I>T No EVA
rs219641773 445 M>T No EVA
rs228397711 448 R>Q No EVA
rs3388941322 466 I>F No EVA
rs3388936350 477 S>P No EVA
rs3388939302 505 V>G No EVA
rs3388945134 543 R>G No EVA
rs3388941716 551 L>P No EVA
rs3388939262 558 K>N No EVA
rs3388945825 566 A>S No EVA
rs3388941715 568 E>D No EVA
rs579137449 574 R>Q No EVA
rs582379148 576 A>Y No EVA

No associated diseases with Q8K0L3

3 regional properties for Q8K0L3

Type Name Position InterPro Accession
domain AMP-dependent synthetase/ligase domain 62 - 469 IPR000873
conserved_site AMP-binding, conserved site 218 - 229 IPR020845
domain AMP-binding enzyme, C-terminal domain 478 - 558 IPR025110

Functions

Description
EC Number 6.2.1.2 Acid--thiol ligases
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
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
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.

7 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
benzoate-CoA ligase activity Catalysis of the reaction: ATP + benzoate + CoA = AMP + benzoyl-CoA + diphosphate.
butyrate-CoA ligase activity Catalysis of the reaction: ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA.
decanoate-CoA ligase activity Catalysis of the reaction: ATP + decanoate + CoA = AMP + diphosphate + decanoyl-CoA.
fatty acid ligase activity Catalysis of the ligation of a fatty acid to an acceptor, coupled to the hydrolysis of ATP.
fatty-acyl-CoA synthase activity Catalysis of the reaction: acetyl-CoA + n malonyl-CoA + 2n NADH + 2n NADPH + 4n H+ = a long-chain acyl-CoA + n CoA + n CO2 + 2n NAD+ + 2n NADP+.
metal ion binding Binding to a metal ion.

2 GO annotations of biological process

Name Definition
acyl-CoA metabolic process The chemical reactions and pathways involving acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with an acyl group.
fatty acid biosynthetic process The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.

8 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9NR19 ACSS2 Acetyl-coenzyme A synthetase, cytoplasmic Homo sapiens (Human) PR
Q08AH3 ACSM2A Acyl-coenzyme A synthetase ACSM2A, mitochondrial Homo sapiens (Human) PR
Q68CK6 ACSM2B Acyl-coenzyme A synthetase ACSM2B, mitochondrial Homo sapiens (Human) PR
Q9QXG4 Acss2 Acetyl-coenzyme A synthetase, cytoplasmic Mus musculus (Mouse) PR
Q9D2R0 Aacs Acetoacetyl-CoA synthetase Mus musculus (Mouse) PR
Q9JMI1 Aacs Acetoacetyl-CoA synthetase Rattus norvegicus (Rat) PR
O70490 Acsm2 Acyl-coenzyme A synthetase ACSM2, mitochondrial Rattus norvegicus (Rat) PR
Q84P17 AAE18 Probable acyl-activating enzyme 18, peroxisomal Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MHHLWKIPRL FTLWGNEISC RTFHMNIKKL IPIQWGHQEA PAKFNFASDV IDHWASVEKA
70 80 90 100 110 120
GKRSSGPALW WMNGSGKEIK WSFRELSEAS KQTANVLSGA CGLHRGDRVA VVLPRIPEWW
130 140 150 160 170 180
LMILGCMRTG LVFMPGTIQM RSSDILYRLQ ASKARAIVAG DEVAQEVDAV APDCSFLKIK
190 200 210 220 230 240
LLVSENSREG WLNFKALLKE ASTIHQCVET ESRESAAIYF TSGTSGPPKM AEHSHCSLGI
250 260 270 280 290 300
KAKMDAASWT GLSTSDIIWT ISDTAWIMNI LGAFLEPWVL GACIFVHLLP KFDSQTVLKV
310 320 330 340 350 360
LSSYPINTLV GAPIIYRMLL QQDLSSYKFP HLHSCFSGGE TLLPETLENW KAKTGLEIRE
370 380 390 400 410 420
IYGQTETGLI CRVSRTMKVK PGYLGTAFAH YDVQVIDEQG NVLPPGKEGD IAIRVKPIWP
430 440 450 460 470 480
IGMFSGYVDN PKKTQDNIRG DFWLMGDRGI KDPEGYFHFI GRSDDIINSS GYRIGPSEVE
490 500 510 520 530 540
NALMEHPAVS ETAVISSPDP SRGEVVKAFV VLAPEFLSHD RDQLTKVLQE HVKSVTAPYK
550 560 570
YPRKVEFVLD LPKTVTGKIE RAKLRAKEWK TSGRA