BIUH_RHIL3
ID BIUH_RHIL3 Reviewed; 233 AA.
AC Q1M7F4;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Biuret amidohydrolase {ECO:0000303|PubMed:29425231};
DE EC=3.5.1.84 {ECO:0000269|PubMed:21897878, ECO:0000269|PubMed:29425231};
DE AltName: Full=Biuret hydrolase {ECO:0000303|PubMed:21897878};
GN Name=biuH {ECO:0000303|PubMed:29425231};
GN ORFNames=pRL100352 {ECO:0000312|EMBL:CAK10578.1};
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OG Plasmid pRL10 {ECO:0000312|EMBL:CAK10578.1}.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841;
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=3841;
RX PubMed=21897878; DOI=10.1021/cs200295n;
RA Cameron S.M., Durchschein K., Richman J.E., Sadowsky M.J., Wackett L.P.;
RT "A new family of biuret hydrolases involved in S-triazine ring
RT metabolism.";
RL ACS Catal. 2011:1075-1082(2011).
RN [3] {ECO:0007744|PDB:5BK6, ECO:0007744|PDB:6AZN, ECO:0007744|PDB:6AZO, ECO:0007744|PDB:6AZQ, ECO:0007744|PDB:6AZS}
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF WILD-TYPE; MUTANTS ALA-142;
RP HIS-142; SER-175 AND MUTANT SER-175 IN COMPLEX WITH BIURET, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, ACTIVE SITES, AND MUTAGENESIS OF ASP-36; PHE-41; LYS-142; LYS-145;
RP CYS-175 AND GLN-215.
RC STRAIN=3841;
RX PubMed=29425231; DOI=10.1371/journal.pone.0192736;
RA Esquirol L., Peat T.S., Wilding M., Lucent D., French N.G., Hartley C.J.,
RA Newman J., Scott C.;
RT "Structural and biochemical characterization of the biuret hydrolase (BiuH)
RT from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv.
RT viciae 3841.";
RL PLoS ONE 13:e0192736-e0192736(2018).
CC -!- FUNCTION: Involved in the degradation of cyanuric acid, an intermediate
CC in the degradation of s-triazide herbicides such as atrazine
CC (PubMed:21897878). Catalyzes the hydrolysis of biuret to urea-1-
CC carboxylate (allophanate) and ammonia (PubMed:21897878,
CC PubMed:29425231). The substrate, biuret, is formed by the spontaneous
CC decarboxylation of carboxybiuret (PubMed:21897878).
CC {ECO:0000269|PubMed:21897878, ECO:0000269|PubMed:29425231}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=biuret + H2O = NH4(+) + urea-1-carboxylate;
CC Xref=Rhea:RHEA:17525, ChEBI:CHEBI:15377, ChEBI:CHEBI:15832,
CC ChEBI:CHEBI:18138, ChEBI:CHEBI:28938; EC=3.5.1.84;
CC Evidence={ECO:0000269|PubMed:21897878, ECO:0000269|PubMed:29425231};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17526;
CC Evidence={ECO:0000269|PubMed:21897878, ECO:0000269|PubMed:29425231};
CC -!- ACTIVITY REGULATION: Strongly inhibited by the sulfhydryl-modifying
CC reagents N-ethylmaleimide and iodoacetamide (PubMed:21897878).
CC Inhibited by the substrate analog N-carbamoyl aspartic acid
CC (PubMed:29425231). {ECO:0000269|PubMed:21897878,
CC ECO:0000269|PubMed:29425231}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23 uM for biuret {ECO:0000269|PubMed:21897878};
CC KM=79 uM for biuret {ECO:0000269|PubMed:29425231};
CC Note=kcat is 4.0 sec(-1) (PubMed:21897878). kcat is 11.9 sec(-1)
CC (PubMed:29425231). {ECO:0000269|PubMed:21897878,
CC ECO:0000269|PubMed:29425231};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:21897878};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:29425231}.
CC -!- SIMILARITY: Belongs to the isochorismatase family. {ECO:0000305}.
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DR EMBL; AM236084; CAK10578.1; -; Genomic_DNA.
DR RefSeq; WP_011654379.1; NC_008381.1.
DR PDB; 5BK6; X-ray; 1.59 A; A/B/C/D=1-233.
DR PDB; 6AZN; X-ray; 1.75 A; A/B/C/D/F/G/H/I=1-233.
DR PDB; 6AZO; X-ray; 2.46 A; A/B/C/D=1-233.
DR PDB; 6AZQ; X-ray; 2.22 A; A/B/C/D/E/F/G/H=1-233.
DR PDB; 6AZS; X-ray; 1.59 A; A/B/C/D=1-233.
DR PDBsum; 5BK6; -.
DR PDBsum; 6AZN; -.
DR PDBsum; 6AZO; -.
DR PDBsum; 6AZQ; -.
DR PDBsum; 6AZS; -.
DR SMR; Q1M7F4; -.
DR EnsemblBacteria; CAK10578; CAK10578; pRL100352.
DR KEGG; rle:pRL100352; -.
DR HOGENOM; CLU_068979_8_0_5; -.
DR OMA; IIIDMQT; -.
DR OrthoDB; 1442962at2; -.
DR BioCyc; MetaCyc:MON-20658; -.
DR BRENDA; 3.5.1.84; 5344.
DR Proteomes; UP000006575; Plasmid pRL10.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.850; -; 1.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR Pfam; PF00857; Isochorismatase; 1.
DR SUPFAM; SSF52499; SSF52499; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Plasmid.
FT CHAIN 1..233
FT /note="Biuret amidohydrolase"
FT /id="PRO_0000455209"
FT ACT_SITE 36
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:29425231"
FT ACT_SITE 142
FT /evidence="ECO:0000305|PubMed:29425231"
FT ACT_SITE 175
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:29425231"
FT BINDING 84
FT /ligand="biuret"
FT /ligand_id="ChEBI:CHEBI:18138"
FT /evidence="ECO:0000269|PubMed:29425231,
FT ECO:0007744|PDB:6AZQ"
FT BINDING 145
FT /ligand="biuret"
FT /ligand_id="ChEBI:CHEBI:18138"
FT /evidence="ECO:0000269|PubMed:29425231,
FT ECO:0007744|PDB:6AZQ"
FT BINDING 170..175
FT /ligand="biuret"
FT /ligand_id="ChEBI:CHEBI:18138"
FT /evidence="ECO:0000269|PubMed:29425231,
FT ECO:0007744|PDB:6AZQ"
FT BINDING 215
FT /ligand="biuret"
FT /ligand_id="ChEBI:CHEBI:18138"
FT /evidence="ECO:0000269|PubMed:29425231,
FT ECO:0007744|PDB:6AZQ"
FT MUTAGEN 36
FT /note="D->A,E,N,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:29425231"
FT MUTAGEN 41
FT /note="F->A: 540-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:29425231"
FT MUTAGEN 41
FT /note="F->L: 713-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:29425231"
FT MUTAGEN 41
FT /note="F->W: 73-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:29425231"
FT MUTAGEN 41
FT /note="F->Y: 138-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:29425231"
FT MUTAGEN 142
FT /note="K->A,H: Loss of activity."
FT /evidence="ECO:0000269|PubMed:29425231"
FT MUTAGEN 142
FT /note="K->R: 297-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:29425231"
FT MUTAGEN 145
FT /note="K->A,H,R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:29425231"
FT MUTAGEN 175
FT /note="C->A,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:29425231"
FT MUTAGEN 215
FT /note="Q->A: 419-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:29425231"
FT MUTAGEN 215
FT /note="Q->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:29425231"
FT MUTAGEN 215
FT /note="Q->E: 1300-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:29425231"
FT MUTAGEN 215
FT /note="Q->N: 38-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:29425231"
SQ SEQUENCE 233 AA; 25540 MW; 29A63B0488251858 CRC64;
MDAMVETNRH FIDADPYPWP YNGALRPDNT ALIIIDMQTD FCGKGGYVDH MGYDLSLVQA
PIEPIKRVLA AMRAKGYHII HTREGHRPDL ADLPANKRWR SQRIGAGIGD PGPCGRILTR
GEPGWDIIPE LYPIEGETII DKPGKGSFCA TDLELVLNQK RIENIILTGI TTDVCVSTTM
REANDRGYEC LLLEDCCGAT DYGNHLAAIK MVKMQGGVFG SVSNSAALVE ALP
