TRIA_ACIAI
ID TRIA_ACIAI Reviewed; 474 AA.
AC Q9EYU0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Melamine deaminase {ECO:0000303|PubMed:11274097};
DE EC=3.5.4.45 {ECO:0000269|PubMed:11274097, ECO:0000269|PubMed:22768133};
GN Name=triA {ECO:0000303|PubMed:11274097};
OS Acidovorax citrulli (Acidovorax avenae subsp. citrulli).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=80869;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND SIMILARITY WITH ATZA.
RC STRAIN=NRRL B-12227;
RX PubMed=11274097; DOI=10.1128/jb.183.8.2405-2410.2001;
RA Seffernick J.L., de Souza M.L., Sadowsky M.J., Wackett L.P.;
RT "Melamine deaminase and atrazine chlorohydrolase: 98 percent identical but
RT functionally different.";
RL J. Bacteriol. 183:2405-2410(2001).
RN [2]
RP FUNCTION IN DEAMINATION OF CAAT.
RC STRAIN=NRRL B-12227;
RX PubMed=12200330; DOI=10.1128/aem.68.9.4672-4675.2002;
RA Seffernick J.L., Shapir N., Schoeb M., Johnson G., Sadowsky M.J.,
RA Wackett L.P.;
RT "Enzymatic degradation of chlorodiamino-s-triazine.";
RL Appl. Environ. Microbiol. 68:4672-4675(2002).
RN [3]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF LEU-84; ASP-328 AND CYS-331.
RX PubMed=22768133; DOI=10.1371/journal.pone.0039822;
RA Noor S., Taylor M.C., Russell R.J., Jermiin L.S., Jackson C.J.,
RA Oakeshott J.G., Scott C.;
RT "Intramolecular epistasis and the evolution of a new enzymatic function.";
RL PLoS ONE 7:E39822-E39822(2012).
CC -!- FUNCTION: Displaces two of the three amino groups from melamine,
CC producing ammeline and ammelide as sequential products
CC (PubMed:11274097). Can also catalyze deamination of other s-triazines
CC such as CAAT (2-chloro-4,6-diamino-s-triazine) and aminoatrazine
CC (PubMed:11274097, PubMed:12200330). Has no activity with ammelide,
CC atrazine, halo-triazine substrates or with pyrimidines
CC (PubMed:11274097). {ECO:0000269|PubMed:11274097,
CC ECO:0000269|PubMed:12200330}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + melamine = ammeline + NH4(+); Xref=Rhea:RHEA:26197,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28646, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:77798; EC=3.5.4.45;
CC Evidence={ECO:0000269|PubMed:11274097, ECO:0000269|PubMed:22768133};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ammeline + H(+) + H2O = ammelide + NH4(+);
CC Xref=Rhea:RHEA:26201, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28134, ChEBI:CHEBI:28646, ChEBI:CHEBI:28938; EC=3.5.4.45;
CC Evidence={ECO:0000269|PubMed:11274097};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P72156};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:P72156};
CC -!- ACTIVITY REGULATION: Melamine catalysis is highly inhibited in the
CC presence of aminoatrazine. {ECO:0000269|PubMed:11274097}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: TriA and atrazine chlorohydrolase (AtzA) from
CC Pseudomonas sp. strain ADP are 98% identical but catalyze distinct
CC biochemical reactions. Enzymes differ by only 9 amino acids. These 9
CC amino acid differences between TriA and AtzA represent a short
CC evolutionary pathway connecting enzymes catalyzing physiologically
CC relevant deamination and dehalogenation reactions, respectively
CC (PubMed:11274097). Potential evolutionary trajectories between AtzA and
CC TriA have been constructed, and catalytic activities of the
CC intermediates along those trajectories have been characterized
CC (PubMed:22768133). {ECO:0000269|PubMed:22768133,
CC ECO:0000305|PubMed:11274097}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ATZ/TRZ family. {ECO:0000305}.
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DR EMBL; AF312304; AAG41202.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9EYU0; -.
DR SMR; Q9EYU0; -.
DR KEGG; ag:AAG41202; -.
DR BioCyc; MetaCyc:MON-12128; -.
DR BRENDA; 3.5.4.45; 12473.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0018756; F:ammeline aminohydrolase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Iron; Metal-binding.
FT CHAIN 1..474
FT /note="Melamine deaminase"
FT /id="PRO_0000378492"
FT BINDING 66
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P72156"
FT BINDING 68
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P72156"
FT BINDING 276
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P72156"
FT BINDING 327
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P72156"
FT SITE 84
FT /note="Major determinant of melamine specificity"
FT /evidence="ECO:0000305|PubMed:22768133"
FT SITE 328
FT /note="Major determinant of melamine specificity"
FT /evidence="ECO:0000305|PubMed:22768133"
FT SITE 331
FT /note="Major determinant of melamine specificity"
FT /evidence="ECO:0000305|PubMed:22768133"
FT MUTAGEN 84
FT /note="L->F: 3.4-fold decrease in catalytic efficiency with
FT melamine. 11.4-fold increase in specificity towards
FT atrazine. High atrazine dechlorinase activity and loss of
FT melamine deaminase activity; when associated with N-328 and
FT S-331."
FT /evidence="ECO:0000269|PubMed:22768133"
FT MUTAGEN 328
FT /note="D->N: Loss of activity. High atrazine dechlorinase
FT activity and loss of melamine deaminase activity; when
FT associated with F-84 and S-331."
FT /evidence="ECO:0000269|PubMed:22768133"
FT MUTAGEN 331
FT /note="C->S: 6.3-fold decrease in catalytic efficiency with
FT melamine. 24.3-fold increase in specificity towards
FT atrazine. High atrazine dechlorinase activity and loss of
FT melamine deaminase activity; when associated with F-84 and
FT N-328."
FT /evidence="ECO:0000269|PubMed:22768133"
SQ SEQUENCE 474 AA; 52606 MW; E07912649D849B72 CRC64;
MQTLSIQHGT LVTMDQYRRV LGDSWVHVQD GRIVALGVHA ESVPPPADRV IDARGKVVLP
GFINAHTHVN QILLRGGPSH GRQLYDWLFN VLYPGQKAMR PEDVAVAVRL YCAEAVRSGI
TTINDNADSA IYPGNIEAAM AVYGEVGVRV VYARMFFDRM DGRIQGYVDA LKARSPQVEL
CSIMEETAVA KDRITALSDQ YHGTAGGRIS VWPAPAITPA VTVEGMRWAQ AFARDRAVMW
TLHMAESDHD ERLHWMSPAE YMECYGLLDE RLQVAHCVYF DRKDVRLLHR HNVKVASQVV
SNAYLGSGVA PVPEMVERGM AVGIGTDDGN CNDSVNMIGD MKFMAHIHRA VHRDADVLTP
EKILEMATID GARSLGMDHE IGSIETGKRA DLILLDLRHP QTTPHHHLAA TIVFQAYGNE
VDTVLIDGNV VMENRRLSFL PPERELAFLE EAQSRATAIL QRANMVANPA WRSL
