Q4WPX2

PR
Gene name
ppoA (AFUA_4G10770)
Protein name
Psi-producing oxygenase A
Names
Fatty acid oxygenase ppoA
Species
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
KEGG Pathway
afm:AFUA_4G10770
EC number
1.13.11.60: With incorporation of two atoms of oxygen
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-52 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q4WPX2

Entry ID Method Resolution Chain Position Source
AF-Q4WPX2-F1 Predicted AlphaFoldDB

No variants for Q4WPX2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q4WPX2

No associated diseases with Q4WPX2

2 regional properties for Q4WPX2

Type Name Position InterPro Accession
conserved_site Cytochrome P450, conserved site 999 - 1008 IPR017972
domain Psi-factor producing oxygenase, N-terminal heme peroxidase domain 98 - 647 IPR034812

Functions

Description
EC Number 1.13.11.60 With incorporation of two atoms 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

9 GO annotations of molecular function

Name Definition
dioxygenase activity Catalysis of an oxidation-reduction (redox) reaction in which both atoms of oxygen from one molecule of O2 are incorporated into the (reduced) product(s) of the reaction. The two atoms of oxygen may be distributed between two different products. [DOI:10.1016/S0040-4020(03)00944-X, GOC:bf]
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
iron ion binding Binding to an iron (Fe) ion.
isomerase activity Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
linoleate 8R-lipoxygenase activity Catalysis of the reaction: O(2) + linoleate = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate.
monooxygenase activity Catalysis of the incorporation of one atom from molecular oxygen into a compound and the reduction of the other atom of oxygen to water.
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from each of two donors, and molecular oxygen is reduced or incorporated into a donor.
oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from one donor, and two oxygen atoms is incorporated into a donor.
peroxidase activity Catalysis of the reaction: a donor + a peroxide = an oxidized donor + 2 H2O.

3 GO annotations of biological process

Name Definition
oxylipin biosynthetic process The chemical reactions and pathways resulting in the formation of any oxylipin, any of a group of biologically active compounds formed by oxidative metabolism of polyunsaturated fatty acids.
prostaglandin biosynthetic process The chemical reactions and pathways resulting in the formation of prostaglandins, any of a group of biologically active metabolites which contain a cyclopentane ring.
response to oxidative stress Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSEKQTGSAN GGLGKTLAQL EQVVSASLRP LPSQTGDGTY VTEQVKTGIL KDLSHVDLGD
70 80 90 100 110 120
LKTLVDVSKS ALTGEALDDR KYIMERVIQL SAGLPSTSQI GKELTNTFLT TLWNDLEHPP
130 140 150 160 170 180
ISYLGRDAMY RRADGSGNNV LWPHIGAAGT PYARSVQPKT VQSPNLPDPE TLFDCLLARK
190 200 210 220 230 240
EYKEHPNKIS SVLFYIASII IHDLFETDRK DPAISLTSSY LDLSPLYGNN QQEQDLIRTF
250 260 270 280 290 300
KDGKLKPDCF STKRVLGFPP DVGVVLIMFN RFHNYVVEKL AMINEGGRFT KPQESDTAAY
310 320 330 340 350 360
AKYDNDLFQT GRLVTCGLYV NIILKDYVRT ILNINRTDSI WSLDPRSEMK DGLLGRAAAQ
370 380 390 400 410 420
ATGNQVAAEF NLVYRWHSCI SQRDQKWTED MYQELFPGQD PSKISLQDFL RGLGRWEAKL
430 440 450 460 470 480
PGEPRERPFA GLQRKADGSY DDNDLVKIFE ESVEDCAGAF GALHVPTVFR SIEALGIQQA
490 500 510 520 530 540
RSWNLATLNE FRKYFNLAPY KTFEEINSDP YVADQLKRLY DHPDRVEIYP GIIVEDAKES
550 560 570 580 590 600
MAPGSGLCTN FTISRAILSD AVALVRGDRF HTVDFTPKHL TNWAYNEIQP QDSVDQTHVF
610 620 630 640 650 660
YKLVLRAFPN HFRGDSIYAH FPLVVPSENK KILTKLGTAD KYSWDRPNYT PPPQFINSHS
670 680 690 700 710 720
ACMSILSDQE TFKVTWGSKI EFLMRHNNQP YGRDFMLSGD RTPNAMSRQM MGKALYRDKW
730 740 750 760 770 780
ETEVKRFYEN ITLKLLHRYS YKLAGVNQVD VVRDIANLAQ VHFCASVFSL PLKTESNPRG
790 800 810 820 830 840
IFTESELYQI MAVVFTSIFY DADIGKSFEL NQAARAVTQQ LGQLTLANVE LIAKTGFIAN
850 860 870 880 890 900
LVNSLHRHDV LSEYGVHMIQ RLLDSGMPAP EIVWTHVLPT AGGMVANQAQ LFSQSLDYYL
910 920 930 940 950 960
SEEGSVHLPE INRLAKEDTT EADDLLLRYF MEGARIRSSV ALPRVVAQPT VVEDNGQKIT
970 980 990 1000 1010 1020
LKQGQHIICN LVSASMDPVT FPEPDKVKLD RDMNLYAHFG FGPHQCLGLG LCKTALTTML
1030 1040 1050 1060 1070
KVIGRLDNLR RAPGGQGKLK KLSGPGGIAM YMTPDQTAFF PFPTTMKIQW DGDLPEVKE