ID A0A2G9H9F5_9LAMI Unreviewed; 450 AA.
AC A0A2G9H9F5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Catechol oxidase {ECO:0000313|EMBL:PIN14146.1};
DE EC=1.10.3.1 {ECO:0000313|EMBL:PIN14146.1};
GN ORFNames=CDL12_13226 {ECO:0000313|EMBL:PIN14146.1};
OS Handroanthus impetiginosus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC Handroanthus.
OX NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN14146.1, ECO:0000313|Proteomes:UP000231279};
RN [1] {ECO:0000313|Proteomes:UP000231279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT forest tree.";
RL Gigascience 7:1-16(2018).
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIN14146.1}.
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DR EMBL; NKXS01002345; PIN14146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9H9F5; -.
DR STRING; 429701.A0A2G9H9F5; -.
DR OrthoDB; 4070889at2759; -.
DR Proteomes; UP000231279; Unassembled WGS sequence.
DR GO; GO:0004097; F:catechol oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 2.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR022740; Polyphenol_oxidase_C.
DR InterPro; IPR022739; Polyphenol_oxidase_cen.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF87; POLYPHENOL OXIDASE CHLOROPLASTIC; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF12142; PPO1_DWL; 1.
DR Pfam; PF12143; PPO1_KFDV; 1.
DR Pfam; PF00264; Tyrosinase; 2.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:PIN14146.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 150..167
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 260..271
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
SQ SEQUENCE 450 AA; 50505 MW; C5FE2BBBE07DCA3E CRC64;
MASPPLPCAL TTTTSAASSH PLFPKPPHFT IHIKRSHRLN VSCTVAQNHN DSSQNVDTSQ
GKVIDRRNML LGLGGLYGAA NLVSTLMRIR PSAHKVSLEY IYKYNLAIDR MKRLPADDPR
NFMQQANIHC TYCNGAYDQP GQGSLDLQVH NSWLFFPFHR SYLYFYERIL GKLIGDPTFA
LPFWNWDNPK CHAPSPRARD VVANNITIMY TKMIRGNSDI YDFMGQAYHK GTAVNPGPGS
SERGSHTTIH VWVGDPRRRD PLFYCHHANV DCMWPLWQYY LPSNKVPDKR ITEPDFLNAS
FLFYDKNARL VPVKVKDTLD NLRMGPSPQT AKAKILRAST TVPKASTLFP LNLDRVFDVL
VNDKDDNALE LDKASYAGIY AQVAHKTTNK TATTTIRLKL TDLYEDMDIN DDDTIVMTFV
PRHQCPGVTI GGVKIIEAPA TTSTTVASSS
//
