ID Q6H237_NICAT Unreviewed; 319 AA.
AC Q6H237;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 85.
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 Name=Aco1 {ECO:0000313|EMBL:AAR99394.1};
GN Synonyms=ACO_2 {ECO:0000313|EMBL:OIT08065.1};
GN ORFNames=A4A49_18038 {ECO:0000313|EMBL:OIT08065.1};
OS Nicotiana attenuata (Coyote tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=49451 {ECO:0000313|EMBL:AAR99394.1};
RN [1] {ECO:0000313|EMBL:AAR99394.1}
RP NUCLEOTIDE SEQUENCE.
RA Winz R.A., Halitschke R., Baldwin I.T.;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAR99394.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15133153; DOI=10.1104/pp.104.040360;
RA Lou Y., Baldwin I.T.;
RT "Nitrogen supply influences herbivore-induced direct and indirect defenses
RT and transcriptional responses in Nicotiana attenuata.";
RL Plant Physiol. 135:496-506(2004).
RN [3] {ECO:0000313|EMBL:OIT08065.1, ECO:0000313|Proteomes:UP000187609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UT {ECO:0000313|Proteomes:UP000187609}, and UT
RC {ECO:0000313|EMBL:OIT08065.1};
RC TISSUE=Leaves {ECO:0000313|EMBL:OIT08065.1};
RA Xu S., Brockmoeller T., Gaquerel E., Navarro A., Kuhl H., Gase K., Ling Z.,
RA Zhou W., Kreitzer C., Stanke M., Tang H., Lyons E., Pandey P., Pandey S.P.,
RA Timmermann B., Baldwin I.T.;
RT "The genome of Nicotiana attenuata.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AY426756; AAR99394.1; -; mRNA.
DR EMBL; MJEQ01037183; OIT08065.1; -; Genomic_DNA.
DR RefSeq; XP_019246952.1; XM_019391407.1.
DR AlphaFoldDB; Q6H237; -.
DR STRING; 49451.Q6H237; -.
DR EnsemblPlants; OIT08065; OIT08065; A4A49_18038.
DR GeneID; 109226594; -.
DR Gramene; OIT08065; OIT08065; A4A49_18038.
DR KEGG; nau:109226594; -.
DR OMA; PAFWHGD; -.
DR OrthoDB; 1057251at2759; -.
DR Proteomes; UP000187609; Chromosome 1.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IEA:UniProt.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009805; P:coumarin biosynthetic process; IEA:UniProt.
DR GO; GO:0002238; P:response to molecule of fungal origin; 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; PTHR47991:SF215; 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 Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW Reference proteome {ECO:0000313|Proteomes:UP000187609};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 153..253
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 319 AA; 35949 MW; 6683587F90411E7B CRC64;
MENFPIINLE KLNGSEKAAT MEMIKDACEN WGFFELVNHG IPHEVMDTVE KLTKGHYKKC
MEQRFKELVA SKGLEGVEAE VTDMDWESTF FLRHLPVANI SEVAGLDDQY REVMRDFAKR
LENLAEELLD LLCENLGLEN GYLKNVFYGS KGPNFGTKVS NYPPCPKPDL IKGLRAHTDA
GGIILLFQDD KVSGLQLLKD GQWIDVPPMR HSIVVNLGDQ LEVITNGKYK SVMHRVIAQK
DGTRMSLASF YNPGSDAVIY PAPALVEKEA AESKQVYPKY VFDDYMKLYA GLKFQAKEPR
FEAMKSIESD VKLDPIATA
//
