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 C3VEQ3

Entry ID Method Resolution Chain Position Source
AF-C3VEQ3-F1 Predicted AlphaFoldDB

No variants for C3VEQ3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C3VEQ3

No associated diseases with C3VEQ3

No regional properties for C3VEQ3

Type Name Position InterPro Accession
No domain, repeats, and functional sites for C3VEQ3

Functions

Description
EC Number 1.13.11.51 With incorporation of two atoms of oxygen
Subcellular Localization
  • Plastid, chloroplast
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
chloroplast A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.

2 GO annotations of molecular function

Name Definition
9-cis-epoxycarotenoid dioxygenase activity Catalysis of the reactions: a 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a 12'-apo-carotenal; 9-cis-violaxanthin + O2 = 2-cis,4-trans-xanthoxin + (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-dihydro-12'-apo-beta-caroten-12'-al; and 9'-cis-neoxanthin + O2 = 2-cis,4-trans-xanthoxin + (3S,5R,6R)-5,6-dihydroxy-6,7-didehydro-5,6-dihydro-12'-apo-beta-caroten-12'-al.
metal ion binding Binding to a metal ion.

1 GO annotations of biological process

Name Definition
abscisic acid biosynthetic process The chemical reactions and pathways resulting in the formation of abscisic acid, 5-(1-hydroxy-2,6,6,trimethyl-4-oxocyclohex-2-en-1-y1)-3-methylpenta-2,4-dienoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MASSMSLFIS SSSNQTVNSD TLRLKQSSKP TNLIHPNPIK LVRSRQVIAG SIQCSTTPNS
70 80 90 100 110 120
FGLDTTSPSP FYPLPPTCPK EIHPEQSAKP SRPSWNLFQR AAAAVLEAVE DNLIQNLLES
130 140 150 160 170 180
GHPLPKTADP AVQIAGNFAP VGEQKPHHDL PVDGRIPPLI NGVYLRNGAN PLFEPVAGHH
190 200 210 220 230 240
FFDGDGMVHA VHLRNGRASY ACRFTETERL KQERAVGRAI FPKAIGELHG HSGIARLLLF
250 260 270 280 290 300
YARGLLGLID HSRGTGVANA GLIYFNNRLL AMSEDDLPYH VRIKPNGDLE TAGRYDFDGQ
310 320 330 340 350 360
LTTTMIAHPK LDPETREFFA LSYDVIKKPY LKYFRFSPCG EKSPDVEIPL PQPTMMHDFA
370 380 390 400 410 420
ITKNFVIIPD QQVVFKLQEM ICGGSPVVYD KEKIARFGVL PKYAIDASEM QWIDVPDCFC
430 440 450 460 470 480
FHLWNSWEEP ETEEVVVIGS CMTPPDSIFN ESEENLQSVL TEIRLNLRTG KSTRRPILRP
490 500 510 520 530 540
GNSQINLEAG MVNRNRLGRR TRFAYLAIAE PWPKVSGFAK VDLASGEIQR FEYGDGGYGG
550 560 570 580 590 600
EPYFVPREGC DREDGGYVLA FVHDEREGSS ELLIMNAADM RLEAAVRLPS RVPYGFYGTF
VSATELHSQA