ID A0A367LFA6_9HYPO Unreviewed; 1294 AA.
AC A0A367LFA6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN ORFNames=L249_1115 {ECO:0000313|EMBL:RCI13077.1};
OS Ophiocordyceps polyrhachis-furcata BCC 54312.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI13077.1, ECO:0000313|Proteomes:UP000253664};
RN [1] {ECO:0000313|EMBL:RCI13077.1, ECO:0000313|Proteomes:UP000253664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI13077.1,
RC ECO:0000313|Proteomes:UP000253664};
RX PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT pathogenicity and host specificity in insect fungi.";
RL BMC Genomics 16:881-881(2015).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU000672};
CC Note=Contains 1 topaquinone per subunit.
CC {ECO:0000256|RuleBase:RU000672};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000256|PIRSR:PIRSR600269-51,
CC ECO:0000256|RuleBase:RU000672}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000256|ARBA:ARBA00007983, ECO:0000256|RuleBase:RU000672}.
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:RCI13077.1}.
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DR EMBL; LKCN02000007; RCI13077.1; -; Genomic_DNA.
DR STRING; 1330021.A0A367LFA6; -.
DR UniPathway; UPA00139; UER00339.
DR Proteomes; UP000253664; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004411; F:homogentisate 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd07000; cupin_HGO_N; 1.
DR CDD; cd05233; SDR_c; 1.
DR Gene3D; 3.10.450.40; -; 2.
DR Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000269; Cu_amine_oxidase.
DR InterPro; IPR015798; Cu_amine_oxidase_C.
DR InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR InterPro; IPR046451; HgmA_C.
DR InterPro; IPR046452; HgmA_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR PANTHER; PTHR10638:SF94; PRIMARY AMINE OXIDASE; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF04209; HgmA_C; 1.
DR Pfam; PF20510; HgmA_N; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000672};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000672}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000672};
KW Reference proteome {ECO:0000313|Proteomes:UP000253664};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 25..287
FT /note="Homogentisate 1,2-dioxygenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20510"
FT DOMAIN 297..399
FT /note="Homogentisate 1,2-dioxygenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04209"
FT DOMAIN 866..1266
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT REGION 1270..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1278..1294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 939
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 1023
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 1023
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 1294 AA; 142499 MW; D83383EA38F61CDF CRC64;
MAVASRGIQQ YAMPTTKFST PEKYEYRNGF GSLHESEAVK DALPVGANSP QQAPHGLYAE
KLSGTAFTAP RHENLQTWAY RILPSASHLN FEPLGKPFSS QPKESLTYVP NQLRWDPFDI
DKGVDWVRGL RLVAGAGDPT MKSGLGIYVY TAGKDMAPKT AMYSSDGEML IVTQTGVLDI
QTELGNLLVR PNEIAVIPRG MKYRVTLPEG PVRGYILELY RGQFTLPELG PIGSNCLANA
RDFQVPVASF DEDTGTEWSI INKFNGQLFV AKQSHTPFDV VAWHGSDIWH KEIPFHLSED
TFRPPWYHRN TMSEFMGLIQ GDYDAKAGGG FRAGGASLHN VMSAHGPDAT TFDQASNAEL
KPQKVGEGSM AFMFESSLML GLTEWGLETC NKVQPEYNRE SCPYQLWIVE MDVPGFALIT
GAASGLGNAC AKAFAREGSA GIALLDINEE GLMKARDEIE GTTRERGTKI FTFHVDVADE
EQVKQAVCEA AGLFGRLDYV VHAAGISAFH QGGVAFAEAE AWNNVVNVNL SGTFFVLRAA
AQIMLKQEPI LSSIDKRPLQ RGSIVAFASV LSVTAHKSVA AYVASKHGVL GLTRSASVDY
AETALSEGQM RKEIFSLIFI FIRVALLSIQ ETNQARDLVL KLHPGAVIDF RTIYLLEPPK
AEVLPFLALE HAGKVTRSTP RPARLAQAKY DVIGGSKAAE YHESVLDLTA AKVVSHEVIP
TDFHAGLTVF EFKKLVECVK ASPLFQEKLK TIKLPPGFEL VVEPWPYGSP DLGDGQTRLF
QCLCFGRNTA SGSKDSNFYG YPIPFIPVMD FRKNEIIRVD EPATGGGSDP LTGRTHKPGI
VDHCGPSEYV PELLPSGTRQ DVKPLTLQQP QGPSFNMSDS SLIEWQKWRM RVTFNPREGV
VIHDIRYDDR DVLYRLSISD MTVPYADPRT PYHRKQAFDF GDGGLGHAVN NLTLGCDCLG
VIKYLDGVLT TDDGSAEVAK NIVCIHEQDN GINWKHTDWR TGRATVTRRR ELVVQFIITL
ANYEYIFAFK FDQAAGIVVE ARATGIVSVV NIDEGKTAPW GNVVSPGALA QNHQHIFCVR
IDPAVDGHKN TLVQEDSLAV PMNERTNPHG NYYEVRQTPI ATSGGIDLAP FSNRVFKVQN
RAKKNPISGK PVGYKITTPP TQLLLADPNS IQAQRALFAK HHLWVTKFKD DELYAGGRHT
LQSRREVGGV ADAAARGDDV LDDDIVLWSV FGLTHNPRVE DWPVMPVEML EVHITPVDFF
TGNPAIDVPS NTDLGSKRVT DDCCENKTPE KPRL
//
