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 P31684

Entry ID Method Resolution Chain Position Source
AF-P31684-F1 Predicted AlphaFoldDB

No variants for P31684

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P31684

No associated diseases with P31684

3 regional properties for P31684

Type Name Position InterPro Accession
domain AMP-dependent synthetase/ligase domain 38 - 445 IPR000873
conserved_site AMP-binding, conserved site 189 - 200 IPR020845
domain AMP-binding enzyme, C-terminal domain 454 - 529 IPR025110

Functions

Description
EC Number 6.2.1.12 Acid--thiol ligases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
4-coumarate-CoA ligase activity Catalysis of the reaction: ATP + 4-coumarate + CoA = AMP + diphosphate + 4-coumaroyl-CoA.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
CoA-ligase activity Catalysis of the reaction: substrate + ATP + CoASH = AMP + diphosphate + substrate-CoA.

1 GO annotations of biological process

Name Definition
phenylpropanoid metabolic process The chemical reactions and pathways involving aromatic derivatives of trans-cinnamic acid.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8VCW8 Acsf2 Medium-chain acyl-CoA ligase ACSF2, mitochondrial Mus musculus (Mouse) PR
P31685 4CL2 4-coumarate--CoA ligase 2 Solanum tuberosum (Potato) PR
Q9LU36 4CL4 4-coumarate--CoA ligase 4 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MPMDTETKQS GDLIFRSKLP DIYIPKHLPL HSYCFENLSE FNSRPCLIDG ANDRIYTYAE
70 80 90 100 110 120
VELTSRKVAV GLNKLGIQQK DTIMILLPNC PEFVFAFIGA SYLGAISTMA NPLFTPAEVV
130 140 150 160 170 180
KQAKASSAKI VITQACFAGK VKDYAIENDL KVICVDSVPE GCVHFSELIQ SDEHEIPDVK
190 200 210 220 230 240
IQPDDVVALP YSSGTTGLPK GVMLTHKGLV TSVAQQVDGE NANLYMHSDD VLMCVLPLFH
250 260 270 280 290 300
IYSLNSVLLC ALRVGAAILI MQKFDIAQFL ELIPKHKVTI GPFVPPIVLA IAKSPLVDNY
310 320 330 340 350 360
DLSSVRTVMS GAAPLGKELE DAVRAKFPNA KLGQGYGMTE AGPVLAMCLA FAKEPFDIKS
370 380 390 400 410 420
GACGTVVRNA EMKIVDPDTG CSLPRNQPGE ICIRGDQIMK GYLNDPEATA RTIEKEGWLH
430 440 450 460 470 480
TGDIGFIDDD DELFIVDRLK ELIKYKGFQV APAELEALLI NHPDISDAAV VPMIDEQAGE
490 500 510 520 530 540
VPVAFVVRSN GSTITEDEVK DFISKQVIFY KRIKRVFFVE TVPKSPSGKI LRKDLRARLA
AGISN