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 O70490

Entry ID Method Resolution Chain Position Source
AF-O70490-F1 Predicted AlphaFoldDB

No variants for O70490

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O70490

No associated diseases with O70490

3 regional properties for O70490

Type Name Position InterPro Accession
domain AMP-dependent synthetase/ligase domain 67 - 468 IPR000873
conserved_site AMP-binding, conserved site 218 - 229 IPR020845
domain AMP-binding enzyme, C-terminal domain 477 - 557 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.

3 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.
medium-chain fatty-acyl-CoA metabolic process The chemical reactions and pathways involving medium-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. A medium-chain fatty acid is a fatty acid with a chain length of between C6 and C12.

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
Q8K0L3 Acsm2 Acyl-coenzyme A synthetase ACSM2, mitochondrial Mus musculus (Mouse) PR
Q9JMI1 Aacs Acetoacetyl-CoA synthetase Rattus norvegicus (Rat) PR
Q84P17 AAE18 Probable acyl-activating enzyme 18, peroxisomal Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MHWLWKIPRL CTFWGTEMFH RTFHMNIKKL MPIQWGHQEV PAKFNFASDV IDHWASLEKA
70 80 90 100 110 120
GKRSPGPALW WMNGSGEELK WNFRELSEIS KQTANVLTGA CGLQRGDRVA VVLPRVPEWW
130 140 150 160 170 180
LVTLGCMRSG LVFMPGTTQM KSTDILYRLQ SSKARAIVAG DEVVQEVDAV APDCSFLKIK
190 200 210 220 230 240
LLVSEKNREG WLNFKALLKD ASPIHQCVET VSQESAAIYF TSGTSGPPKM AEHSHCSLGL
250 260 270 280 290 300
KAKMDAGWTG LGPSDTMWTI SDTGWILNIL GSFLEPWVLG TCIFVHLLPK FDPQTVLKVL
310 320 330 340 350 360
SSYPINTLLG APLIYRMLLQ QDLSSYKFPH LHSCFSGGET LLPETLESWK AKTGLEIREI
370 380 390 400 410 420
YGQTETGITC RVSRTMKVKP GYLGTAIVPY DVQVIDEQGN VLPPGKEGDM ALRVKPIRPI
430 440 450 460 470 480
GMFSGYVDNP KKTQANIRGD FWLLGDRGIK DTEGYFHFMG RTDDIINSSG YRIGPSEVEN
490 500 510 520 530 540
ALMEHPAVVE TAVISSPDPI RREVVKAFVV LAPEFLSHDQ DQLTKVLQEH VKSVTAPYKY
550 560 570
PRKVEFVLDL PKTITGKIER AKLRAKEWKT SG