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Database: UniProt
Entry: A0A4S8J9B3_MUSBA
LinkDB: A0A4S8J9B3_MUSBA
Original site: A0A4S8J9B3_MUSBA 
ID   A0A4S8J9B3_MUSBA        Unreviewed;       317 AA.
AC   A0A4S8J9B3;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=aminocyclopropanecarboxylate oxidase {ECO:0000256|ARBA:ARBA00039090};
DE            EC=1.14.17.4 {ECO:0000256|ARBA:ARBA00039090};
DE   AltName: Full=Ethylene-forming enzyme {ECO:0000256|ARBA:ARBA00041616};
GN   ORFNames=C4D60_Mb03t12280 {ECO:0000313|EMBL:THU58257.1};
OS   Musa balbisiana (Banana).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Musa.
OX   NCBI_TaxID=52838 {ECO:0000313|EMBL:THU58257.1, ECO:0000313|Proteomes:UP000317650};
RN   [1] {ECO:0000313|EMBL:THU58257.1, ECO:0000313|Proteomes:UP000317650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DH-PKW {ECO:0000313|Proteomes:UP000317650};
RC   TISSUE=Leaves {ECO:0000313|EMBL:THU58257.1};
RA   Yao X.;
RT   "Genome sequencing of Musa balbisiana reveals subgenome evolution and
RT   function divergence in polyploid bananas.";
RL   Nat. Plants 0:0-0(2019).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-aminocyclopropane-1-carboxylate + L-ascorbate + O2 = CO2 +
CC         ethene + 2 H2O + hydrogen cyanide + L-dehydroascorbate;
CC         Xref=Rhea:RHEA:23640, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:18153, ChEBI:CHEBI:18407,
CC         ChEBI:CHEBI:38290, ChEBI:CHEBI:58360, ChEBI:CHEBI:58539;
CC         EC=1.14.17.4; Evidence={ECO:0000256|ARBA:ARBA00036392};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC       methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00037892}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
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:THU58257.1}.
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DR   EMBL; PYDT01000006; THU58257.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4S8J9B3; -.
DR   STRING; 52838.A0A4S8J9B3; -.
DR   Proteomes; UP000317650; Chromosome 3.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-KW.
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; PTHR47991:SF42; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47991; OXOGLUTARATE/IRON-DEPENDENT DIOXYGENASE; 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   Ethylene biosynthesis {ECO:0000256|ARBA:ARBA00022666};
KW   Fruit ripening {ECO:0000256|ARBA:ARBA00033478};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003682};
KW   Metal-binding {ECO:0000256|RuleBase:RU003682};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003682};
KW   Reference proteome {ECO:0000313|Proteomes:UP000317650}.
FT   DOMAIN          154..254
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   317 AA;  36084 MW;  6C49278D80F84285 CRC64;
     MDCSFPVINM EKLQGGEREK AMELLRDACE NWGFFELLNH GISPELMDEV ERLTKEHYRK
     CREQKFKEFA SKALENGSKS EVTDMDWEST FFLRHLPVSN MSELVDMGDD YRKVMKEFAA
     KLEMLAERLL DLLCENLGLE KGYLKKAFCG SKGPSFGTKV SSYPPCPRPE LIKGLRAHTD
     AGGIILLFQD DRVSGLQLLK DDQWIDVPPM RHSIVVNLGD QLEVFTNGKY KSVLHRVVAQ
     TDGNRMSIAS FYNPGSDAVV FPAPSLVQKE AEKDDVAAVY PRFVFEDYMK LYVIQKFQAK
     EPRFEAMKAM ALPIPTS
//
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