BAH1_NOCSJ
ID BAH1_NOCSJ Reviewed; 371 AA.
AC A1SGT4;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Barbiturase 1 {ECO:0000255|HAMAP-Rule:MF_01989};
DE EC=3.5.2.1 {ECO:0000255|HAMAP-Rule:MF_01989, ECO:0000269|PubMed:28235873};
DE AltName: Full=Barbituric acid hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_01989};
DE Short=BAH 1 {ECO:0000255|HAMAP-Rule:MF_01989};
GN OrderedLocusNames=Noca_1505;
OS Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC Nocardioides.
OX NCBI_TaxID=196162;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-499 / JS614;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28235873; DOI=10.1128/aem.03365-16;
RA Peat T.S., Balotra S., Wilding M., Hartley C.J., Newman J., Scott C.;
RT "High resolution X-ray structures of two functionally distinct members of
RT the cyclic amide hydrolase (CyAH) family of Toblerone fold enzymes.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
CC -!- FUNCTION: Responsible for the hydrolysis of barbituric acid (2,4,6-
CC trihydroxy-1,3-pyrimidine), an intermediate in the oxidative catabolism
CC of pyrimidines. Catalyzes the hydrolytic opening of the pyrimidine ring
CC of barbituric acid to yield ureidomalonic acid. {ECO:0000255|HAMAP-
CC Rule:MF_01989, ECO:0000269|PubMed:28235873}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=barbiturate + H2O = 3-oxo-3-ureidopropanoate;
CC Xref=Rhea:RHEA:18653, ChEBI:CHEBI:15377, ChEBI:CHEBI:58775,
CC ChEBI:CHEBI:77938; EC=3.5.2.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01989, ECO:0000269|PubMed:28235873};
CC -!- ACTIVITY REGULATION: Inhibited by cyanuric acid. {ECO:0000255|HAMAP-
CC Rule:MF_01989}.
CC -!- PATHWAY: Pyrimidine metabolism; uracil degradation via oxidative
CC pathway; malonate and urea from uracil: step 2/3. {ECO:0000255|HAMAP-
CC Rule:MF_01989}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01989}.
CC -!- DOMAIN: The monomer structure is formed from three repeating units
CC (RUs) that share the same structure as one another. The monomer and the
CC active site possess nearly threefold rotational symmetry, to the extent
CC that the active site possesses three potential Ser-Lys catalytic dyads,
CC but one of the 3 active site surfaces varies in composition suggesting
CC it is involved in confering substrate specificity. {ECO:0000255|HAMAP-
CC Rule:MF_01989}.
CC -!- SIMILARITY: Belongs to the cyclic amide hydrolase (CyAH) family.
CC {ECO:0000255|HAMAP-Rule:MF_01989}.
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DR EMBL; CP000509; ABL81019.1; -; Genomic_DNA.
DR RefSeq; WP_011754967.1; NC_008699.1.
DR AlphaFoldDB; A1SGT4; -.
DR SMR; A1SGT4; -.
DR STRING; 196162.Noca_1505; -.
DR EnsemblBacteria; ABL81019; ABL81019; Noca_1505.
DR KEGG; nca:Noca_1505; -.
DR eggNOG; ENOG502Z8BS; Bacteria.
DR HOGENOM; CLU_808206_0_0_11; -.
DR OMA; GRYRIGH; -.
DR OrthoDB; 984718at2; -.
DR UniPathway; UPA00582; UER00644.
DR Proteomes; UP000000640; Chromosome.
DR GO; GO:0047694; F:barbiturase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006212; P:uracil catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1330.160; -; 1.
DR Gene3D; 3.30.1330.170; -; 1.
DR Gene3D; 3.30.1330.180; -; 1.
DR HAMAP; MF_01989; Cyc_amidohydrol; 1.
DR InterPro; IPR014086; AtzD/Barbiturase.
DR InterPro; IPR043008; AtzD/Barbiturase_RUA.
DR InterPro; IPR043006; AtzD/Barbiturase_RUB.
DR InterPro; IPR043007; AtzD/Barbiturase_RUC.
DR Pfam; PF09663; Amido_AtzD_TrzD; 1.
DR TIGRFAMs; TIGR02714; amido_AtzD_TrzD; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..371
FT /note="Barbiturase 1"
FT /id="PRO_0000439907"
FT REGION 1..103
FT /note="RU A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 115..250
FT /note="RU B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 256..371
FT /note="RU C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 165
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 233
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8RSQ2, ECO:0000255|HAMAP-
FT Rule:MF_01989"
FT BINDING 82..83
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8RSQ2, ECO:0000255|HAMAP-
FT Rule:MF_01989"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8RSQ2, ECO:0000255|HAMAP-
FT Rule:MF_01989"
FT BINDING 233..234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8RSQ2, ECO:0000255|HAMAP-
FT Rule:MF_01989"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8RSQ2, ECO:0000255|HAMAP-
FT Rule:MF_01989"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8RSQ2, ECO:0000255|HAMAP-
FT Rule:MF_01989"
FT BINDING 350..351
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8RSQ2, ECO:0000255|HAMAP-
FT Rule:MF_01989"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8RSQ2, ECO:0000255|HAMAP-
FT Rule:MF_01989"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8RSQ2, ECO:0000255|HAMAP-
FT Rule:MF_01989"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8RSQ2, ECO:0000255|HAMAP-
FT Rule:MF_01989"
FT BINDING 358
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8RSQ2, ECO:0000255|HAMAP-
FT Rule:MF_01989"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8RSQ2, ECO:0000255|HAMAP-
FT Rule:MF_01989"
FT SITE 327
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
SQ SEQUENCE 371 AA; 39259 MW; 87E662E39A77CFAB CRC64;
MPDAIEVRKV PIHSVADASE LAKLIDDGVM QAERVIAIIG KTEGNGGVND YTRIIADRAF
REVLVEKGAP AEQVKQVPIV WSGGTDGVIS PHATIFATVP PEDLTGALAP SDEQRLTVGF
AMSERLAPED IGRTAMITKV ADAVKVAMER AGISDPADVH YVQTKTPLLT IHTIRDAKSR
GKTVWTEHTH ESMDLSNGCT ALGIAVALGE IEMPSDEDVM HDRSLYSSVA SCSSGVELDQ
AQVVVVGNAP GVGGRYRIGH SVMKDALDQD GIWEAIKDAG LDLPERPRTS DLDGRLVNVF
LKCEASQDGL VRGRRNAMLD DSDVHWHRQI KSCVGGVTAA VTGDPAVFVS VSAAHQGPDG
GGPVAAIVDL G
