BAH2_NOCSJ
ID BAH2_NOCSJ Reviewed; 371 AA.
AC A1SPN2;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Barbiturase 2 {ECO:0000255|HAMAP-Rule:MF_01989};
DE EC=3.5.2.1 {ECO:0000255|HAMAP-Rule:MF_01989};
DE AltName: Full=Barbituric acid hydrolase 2 {ECO:0000255|HAMAP-Rule:MF_01989};
DE Short=BAH 2 {ECO:0000255|HAMAP-Rule:MF_01989};
GN OrderedLocusNames=Noca_4270;
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. Can also use cyanuric
CC acid as a substrate, albeit with lower efficiency. {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};
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; ABL83767.1; -; Genomic_DNA.
DR RefSeq; WP_011757696.1; NC_008699.1.
DR AlphaFoldDB; A1SPN2; -.
DR SMR; A1SPN2; -.
DR STRING; 196162.Noca_4270; -.
DR EnsemblBacteria; ABL83767; ABL83767; Noca_4270.
DR KEGG; nca:Noca_4270; -.
DR eggNOG; ENOG502Z8BS; Bacteria.
DR HOGENOM; CLU_808206_0_0_11; -.
DR OMA; YAMSEVL; -.
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 2"
FT /id="PRO_0000439908"
FT REGION 1..104
FT /note="RU A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 112..247
FT /note="RU B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT REGION 253..371
FT /note="RU C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 162
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT ACT_SITE 230
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 83..84
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 230..231
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 330
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 349..350
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
FT SITE 326
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01989"
SQ SEQUENCE 371 AA; 39465 MW; 93EDE133CFFD0497 CRC64;
MTRPIEVRKV PIEHVSDAAG LADLIDAGVF SADDVIAVVG KTEGNGGVND YTRIISTHAY
RAVLEEKGTR SKEEVAQVPL VWSGGTDGVI SPHATIFAYA PEGRYLPTDE PRVTVGYAMS
EVLLPEDIGR PAMVEKVAAG VRVAMERAGI TDPADVHYVQ TKTPLLVQDT INDAERRGET
VYTHNTLESM DVSNATTALG IAVALGEIEM PTAEQIFHDL SLYSSVASCS SGVELDQAQI
VVVGNARGVG GRFRVGHSIM KDALDMDGVW AAIRDAGLDD MPVDCIHPRH IKGRLVNLFL
KCEADPTGRV RGRRNIMLDD SDVAWHRQIK ACVGGVVAAV SGDPMNFVSV AAVHQGPSGG
GPVIAIVDLE A
