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

3 structures for P15245

Entry ID Method Resolution Chain Position Source
1FOH X-ray 240 A A/B/C/D 2-665 PDB
1PN0 X-ray 170 A A/B/C/D 1-665 PDB
AF-P15245-F1 Predicted AlphaFoldDB

No variants for P15245

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P15245

No associated diseases with P15245

2 regional properties for P15245

Type Name Position InterPro Accession
domain FAD-binding domain 8 - 416 IPR002938
domain Phenol hydroxylase, C-terminal dimerisation domain 452 - 614 IPR012941

Functions

Description
EC Number 1.14.13.7 With NADH or NADPH as one donor, and incorporation of one atom of oxygen
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

2 GO annotations of molecular function

Name Definition
FAD binding Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
phenol 2-monooxygenase activity Catalysis of the reaction: phenol + NADPH + H+ + O2 = catechol + NADP+ + H2O.

1 GO annotations of biological process

Name Definition
phenol-containing compound catabolic process The chemical reactions and pathways resulting in the breakdown of a phenol, any compound containing one or more hydroxyl groups directly attached to an aromatic carbon ring.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTKYSESYCD VLIVGAGPAG LMAARVLSEY VRQKPDLKVR IIDKRSTKVY NGQADGLQCR
70 80 90 100 110 120
TLESLKNLGL ADKILSEAND MSTIALYNPD ENGHIRRTDR IPDTLPGISR YHQVVLHQGR
130 140 150 160 170 180
IERHILDSIA EISDTRIKVE RPLIPEKMEI DSSKAEDPEA YPVTMTLRYM SDHESTPLQF
190 200 210 220 230 240
GHKTENSLFH SNLQTQEEED ANYRLPEGKE AGEIETVHCK YVIGCDGGHS WVRRTLGFEM
250 260 270 280 290 300
IGEQTDYIWG VLDAVPASNF PDIRSPCAIH SAESGSIMII PRENNLVRFY VQLQARAEKG
310 320 330 340 350 360
GRVDRTKFTP EVVIANAKKI FHPYTFDVQQ LDWFTAYHIG QRVTEKFSKD ERVFIAGDAC
370 380 390 400 410 420
HTHSPKAGQG MNTSMMDTYN LGWKLGLVLT GRAKRDILKT YEEERHAFAQ ALIDFDHQFS
430 440 450 460 470 480
RLFSGRPAKD VADEMGVSMD VFKEAFVKGN EFASGTAINY DENLVTDKKS SKQELAKNCV
490 500 510 520 530 540
VGTRFKSQPV VRHSEGLWMH FGDRLVTDGR FRIIVFAGKA TDATQMSRIK KFSAYLDSEN
550 560 570 580 590 600
SVISLYTPKV SDRNSRIDVI TIHSCHRDDI EMHDFPAPAL HPKWQYDFIY ADCDSWHHPH
610 620 630 640 650 660
PKSYQAWGVD ETKGAVVVVR PDGYTSLVTD LEGTAEIDRY FSGILVEPKE KSGAQTEADW
TKSTA