RUTB_AZOC5
ID RUTB_AZOC5 Reviewed; 227 AA.
AC A8IAC9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Ureidoacrylate amidohydrolase RutB {ECO:0000255|HAMAP-Rule:MF_00830};
DE EC=3.5.1.110 {ECO:0000255|HAMAP-Rule:MF_00830};
GN Name=rutB {ECO:0000255|HAMAP-Rule:MF_00830}; OrderedLocusNames=AZC_2493;
OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS 6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Azorhizobium.
OX NCBI_TaxID=438753;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC 13405 / ORS 571;
RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT caulinodans ORS571.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes ureidoacrylate to form aminoacrylate and
CC carbamate. The carbamate hydrolyzes spontaneously, thereby releasing
CC one of the nitrogen atoms of the pyrimidine ring as ammonia and one of
CC its carbon atoms as CO2. {ECO:0000255|HAMAP-Rule:MF_00830}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(Z)-3-ureidoacrylate + H(+) + H2O = (Z)-3-aminoacrylate + CO2
CC + NH4(+); Xref=Rhea:RHEA:42624, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:28938, ChEBI:CHEBI:59891,
CC ChEBI:CHEBI:59894; EC=3.5.1.110; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00830};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(Z)-3-ureidoacrylate + H2O = (Z)-3-aminoacrylate + carbamate +
CC H(+); Xref=Rhea:RHEA:31603, ChEBI:CHEBI:13941, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:59891, ChEBI:CHEBI:59894;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00830};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(Z)-2-methylureidoacrylate + H(+) + H2O = (Z)-2-
CC methylaminoacrylate + CO2 + NH4(+); Xref=Rhea:RHEA:42620,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:143783, ChEBI:CHEBI:145735;
CC EC=3.5.1.110; Evidence={ECO:0000255|HAMAP-Rule:MF_00830};
CC -!- SIMILARITY: Belongs to the isochorismatase family. RutB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00830}.
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DR EMBL; AP009384; BAF88491.1; -; Genomic_DNA.
DR AlphaFoldDB; A8IAC9; -.
DR SMR; A8IAC9; -.
DR STRING; 438753.AZC_2493; -.
DR EnsemblBacteria; BAF88491; BAF88491; AZC_2493.
DR KEGG; azc:AZC_2493; -.
DR eggNOG; COG1335; Bacteria.
DR HOGENOM; CLU_068979_8_0_5; -.
DR OMA; WHKSNAL; -.
DR Proteomes; UP000000270; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-UniRule.
DR GO; GO:0019740; P:nitrogen utilization; IEA:UniProtKB-UniRule.
DR GO; GO:0006212; P:uracil catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.850; -; 1.
DR HAMAP; MF_00830; RutB; 1.
DR InterPro; IPR000868; Isochorismatase-like.
DR InterPro; IPR036380; Isochorismatase-like_sf.
DR InterPro; IPR019916; RutB.
DR Pfam; PF00857; Isochorismatase; 1.
DR SUPFAM; SSF52499; SSF52499; 1.
DR TIGRFAMs; TIGR03614; RutB; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..227
FT /note="Ureidoacrylate amidohydrolase RutB"
FT /id="PRO_0000402648"
FT ACT_SITE 22
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
FT ACT_SITE 131
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
FT ACT_SITE 164
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00830"
SQ SEQUENCE 227 AA; 24689 MW; AEC7651D22B3B7A1 CRC64;
MLPARPEPLS VAVEETAVVV VDMQNAYASP GGYLDIAGFD ISGAKAAISA IAETVEAARA
AGVTVIYFQN GWDKDYVEAG GPGSPNWHKS NALKTMRKKP ELQGQLLAKG GWDYALVDQL
APQPGDIVVP KPRYSGFFNS QFDSILRARG IRNLVFCGIA TNVCVESTLR DGFHLEYFGI
LLEDATHQAG PEYVQKAAIY NVETFFGWVS TVADFRRAFA QIPPKED