RIDA_DERFA
ID RIDA_DERFA Reviewed; 128 AA.
AC A0A1J1DL12;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2017, sequence version 1.
DT 25-MAY-2022, entry version 11.
DE RecName: Full=2-iminobutanoate/2-iminopropanoate deaminase {ECO:0000305};
DE EC=3.5.99.10 {ECO:0000305|PubMed:27539850};
DE AltName: Full=Allergen Der f 34 {ECO:0000303|PubMed:27539850};
DE AltName: Full=Enamine/imine deaminase {ECO:0000303|PubMed:27539850, ECO:0000312|EMBL:BAV90601.1};
DE AltName: Allergen=Der f 34.0101 {ECO:0000305};
GN Name=MAG133 {ECO:0000303|PubMed:27539850, ECO:0000312|EMBL:BAV90601.1};
OS Dermatophagoides farinae (American house dust mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Pyroglyphidae; Dermatophagoidinae; Dermatophagoides.
OX NCBI_TaxID=6954 {ECO:0000312|EMBL:BAV90601.1};
RN [1] {ECO:0000312|EMBL:BAV90601.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-9, FUNCTION,
RP IDENTIFICATION BY MASS SPECTROMETRY, ALLERGEN, AND MUTAGENESIS OF TYR-19;
RP GLY-33; ASN-59; ASN-91; ARG-105; PRO-114 AND GLU-120.
RX PubMed=27539850; DOI=10.1074/jbc.m116.728006;
RA ElRamlawy K.G., Fujimura T., Baba K., Kim J.W., Kawamoto C., Isobe T.,
RA Abe T., Hodge-Hanson K., Downs D.M., Refaat I.H., Beshr Al-Azhary D.,
RA Aki T., Asaoku Y., Hayashi T., Katsutani T., Tsuboi S., Ono K.,
RA Kawamoto S.;
RT "Der f 34, a Novel Major House Dust Mite Allergen Belonging to a Highly
RT Conserved Rid/YjgF/YER057c/UK114 Family of Imine Deaminases.";
RL J. Biol. Chem. 291:21607-21615(2016).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of enamine/imine
CC intermediates that form during the course of normal metabolism
CC (PubMed:27539850). May facilitate the release of ammonia from these
CC potentially toxic reactive metabolites, reducing their impact on
CC cellular components. It may act on enamine/imine intermediates formed
CC by several types of pyridoxal-5'-phosphate-dependent dehydratases
CC including L-threonine dehydratase (By similarity). Preferentially
CC digests Leu and Met in cooperation with L-amino acid oxidase, but
CC digests Phe poorly (PubMed:27539850). {ECO:0000250|UniProtKB:P52758,
CC ECO:0000269|PubMed:27539850}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-iminobutanoate + H2O = 2-oxobutanoate + NH4(+);
CC Xref=Rhea:RHEA:39975, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:76545; EC=3.5.99.10;
CC Evidence={ECO:0000305|PubMed:27539850};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-iminopropanoate + H2O = NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:40671, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:44400; EC=3.5.99.10;
CC Evidence={ECO:0000305|PubMed:27539850};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52758}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 68% of
CC the 19 patients tested allergic to house dust mite (HDM).
CC {ECO:0000269|PubMed:27539850}.
CC -!- SIMILARITY: Belongs to the RutC family. {ECO:0000305}.
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DR EMBL; LC120618; BAV90601.1; -; mRNA.
DR AlphaFoldDB; A0A1J1DL12; -.
DR SMR; A0A1J1DL12; -.
DR Allergome; 11968; Der f 34.
DR Allergome; 11969; Der f 34.0101.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0120242; F:2-iminobutanoate deaminase activity; IEA:RHEA.
DR GO; GO:0120243; F:2-iminopropanoate deaminase activity; IEA:RHEA.
DR GO; GO:0019239; F:deaminase activity; IDA:UniProtKB.
DR GO; GO:1901565; P:organonitrogen compound catabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.1330.40; -; 1.
DR InterPro; IPR006056; RidA.
DR InterPro; IPR019897; RidA_CS.
DR InterPro; IPR035959; RutC-like_sf.
DR InterPro; IPR006175; YjgF/YER057c/UK114.
DR PANTHER; PTHR11803; PTHR11803; 1.
DR Pfam; PF01042; Ribonuc_L-PSP; 1.
DR SUPFAM; SSF55298; SSF55298; 1.
DR TIGRFAMs; TIGR00004; TIGR00004; 1.
DR PROSITE; PS01094; UPF0076; 1.
PE 1: Evidence at protein level;
KW Allergen; Cytoplasm; Direct protein sequencing; Hydrolase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:27539850"
FT CHAIN 2..128
FT /note="2-iminobutanoate/2-iminopropanoate deaminase"
FT /evidence="ECO:0000305|PubMed:27539850"
FT /id="PRO_0000447664"
FT MUTAGEN 19
FT /note="Y->A: Loss of imine deaminase activity; when
FT associated with A-33; A-59; A-91; A-105; A-114 and A-120."
FT /evidence="ECO:0000269|PubMed:27539850"
FT MUTAGEN 33
FT /note="G->A: Loss of imine deaminase activity; when
FT associated with A-19; A-59; A-91; A-105; A-114 and A-120."
FT /evidence="ECO:0000269|PubMed:27539850"
FT MUTAGEN 59
FT /note="N->A: Loss of imine deaminase activity; when
FT associated with A-19; A-33; A-91; A-105; A-114 and A-120."
FT /evidence="ECO:0000269|PubMed:27539850"
FT MUTAGEN 91
FT /note="N->A: Loss of imine deaminase activity; when
FT associated with A-19; A-33; A-59; A-105; A-114 and A-120."
FT /evidence="ECO:0000269|PubMed:27539850"
FT MUTAGEN 105
FT /note="R->A: Loss of imine deaminase activity; when
FT associated with A-19; A-33; A-59; A-91; A-114 and A-120."
FT /evidence="ECO:0000269|PubMed:27539850"
FT MUTAGEN 114
FT /note="P->A: Loss of imine deaminase activity; when
FT associated with A-19; A-33; A-59; A-91; A-105 and A-120."
FT /evidence="ECO:0000269|PubMed:27539850"
FT MUTAGEN 120
FT /note="E->A: Loss of imine deaminase activity; when
FT associated with A-19; A-33; A-59; A-91; A-105 and A-114."
FT /evidence="ECO:0000269|PubMed:27539850"
SQ SEQUENCE 128 AA; 13998 MW; 8566EC40EEAFE374 CRC64;
MSPKRIISTP LAPQPIGPYS QAVQVGNTVY LSGQIGMNVR TNEMVTGPIR DEAQQAFTNM
KAVVEASGAK MSDVVKVNIF IRNFNDFPAI NDVMKEFFQS PFPARSTVGV AELPKNARVE
IESIVVIE
