ID A8IM33_MUSAC Unreviewed; 318 AA. AC A8IM33; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 02-OCT-2024, entry version 69. 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}; OS Musa acuminata (Banana) (Musa cavendishii). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Musaceae; Musa. OX NCBI_TaxID=4641 {ECO:0000313|EMBL:ABW20470.1}; RN [1] {ECO:0000313|EMBL:ABW20470.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Fruit pulp {ECO:0000313|EMBL:ABW20470.1}; RA Roy Choudhury S., Roy S., Sengupta D.N.; RT "Characterization of transcriptional profiles of MA-ACS1 and MA-ACO1 genes RT in response to ethylene, auxin, wounding, cold and different photoperiods RT during ripening in banana fruit."; RL J. Plant Physiol. 165:1865-1878(2008). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU169208; ABW20470.1; -; mRNA. DR AlphaFoldDB; A8IM33; -. 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 GO; GO:0009835; P:fruit ripening; 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 InterPro; IPR050295; Plant_2OG-oxidoreductases. 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 2: Evidence at transcript level; 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}. FT DOMAIN 153..253 FT /note="Fe2OG dioxygenase" FT /evidence="ECO:0000259|PROSITE:PS51471" SQ SEQUENCE 318 AA; 36058 MW; E22E4DE8A98E50BF CRC64; MDSFPVIDME ELLGRERGAA MEILRDACEQ WGFFEILNHG ISHDLMDKVE KVNKEQYNKC REQKFNEFAN KALENADSEI DHLDWESTFF QRHLPVSNIS EIPDLDDQYR KAMKQFAAAI EKLAERLLDL LGANLELEKG YLKKAFSNGS KGPTFGTKVR SYPPCPRPDL VKGLRAHTDA GGIILLFQDD QISGLQFLKD GEWLDVPPMG HAIVVNLGDQ LEVITNGKYK SVVHRVVAQT DGNRMSIASF YNPGSDTVIF PAPALVEKEA EEKKEVYPRF VFEDYMKLYV GHKFRAKEPR FEAMKAMEAV ATHPIATS //