ID   A0A194VDS3_9PEZI        Unreviewed;       359 AA.
AC   A0A194VDS3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=1-aminocyclopropane-1-carboxylate oxidase {ECO:0000313|EMBL:KUI62039.1};
GN   ORFNames=VP1G_09198 {ECO:0000313|EMBL:KUI62039.1};
OS   Valsa mali var. pyri (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI62039.1, ECO:0000313|Proteomes:UP000078576};
RN   [1] {ECO:0000313|Proteomes:UP000078576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
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DR   EMBL; KN714797; KUI62039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194VDS3; -.
DR   STRING; 694573.A0A194VDS3; -.
DR   OrthoDB; 1332763at2759; -.
DR   Proteomes; UP000078576; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47990:SF27; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|RuleBase:RU003682};
KW   Metal-binding {ECO:0000256|RuleBase:RU003682};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078576}.
FT   DOMAIN          204..317
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   359 AA;  40244 MW;  0C025C9DA77B4DC4 CRC64;
     MKQPNPQIDT EARRIPTVDV SPFFSGSQDL STLSTQRLKS AKLLVEALHS FGFAKVTGHG
     LSYNDVSEAI GWVQKLFDLP FDEKMKAPHP PGPMPHRGYS GIGEEKVYSQ EDVDAHARSG
     NADVSQELRK ISDFKESYEI GSENDPVQQN IWLPEGVLPG FREYETSLYG RLADISRTLL
     EAIGVGLGFD SKANEALSEL MSDRHCQLRL LHYPAVSKIQ LQKQLLARLP PHRDWGTITL
     LFQDNRGGLE LKDAKTGRYL HAEPEEGAFV VNVGDMLQRF SNDYFVSALH QVTVPDSAEV
     PDLGLPARYS IPFFVAPDFS HTISTLSHFV SKENPAKYEP VRFDQYGELI SKYQYQSES
//