ID Q2K532_RHIEC Unreviewed; 395 AA.
AC Q2K532;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=N-carbamoyl-beta-alanine amidohydrolase protein {ECO:0000313|EMBL:ABC92054.1};
DE EC=3.5.1.6 {ECO:0000313|EMBL:ABC92054.1};
GN Name=amaB {ECO:0000313|EMBL:ABC92054.1};
GN OrderedLocusNames=RHE_CH03290 {ECO:0000313|EMBL:ABC92054.1};
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC92054.1, ECO:0000313|Proteomes:UP000001936};
RN [1] {ECO:0000313|EMBL:ABC92054.1, ECO:0000313|Proteomes:UP000001936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001235-1};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR001235-
CC 1};
CC -!- SIMILARITY: Belongs to the peptidase M20 family.
CC {ECO:0000256|ARBA:ARBA00006153}.
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DR EMBL; CP000133; ABC92054.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2K532; -.
DR KEGG; ret:RHE_CH03290; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_024588_2_1_5; -.
DR Proteomes; UP000001936; Chromosome.
DR GO; GO:0003837; F:beta-ureidopropionase activity; IEA:UniProtKB-EC.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03884; M20_bAS; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010158; Amidase_Cbmase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01879; hydantase; 1.
DR PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABC92054.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001936};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 194..291
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 395 AA; 42356 MW; 0658A587067F441D CRC64;
MAKIGPGVAG GNNRQTLTDS DAEGRSLFKK WCDEAGLTMG VDQMGTMFAT RPGTDPDALP
VYVGSHLDTQ PTGGKYDGVL GVLSALEVVR TMNDLGIKTK HPIVVTNWTN EEGARFAPAM
LASGVFAGVH SLDFAYNRKD PEGNLFGDEL KRIGWVGDEE VGARKMHAYF EYHIEQGPIL
EAESKQIGVV THCQGLWWLE FTLTGKEAHT GSTPMNMRVN AGLAMSRILE MVQAVAMGEQ
PGAVGGVGQV FFSPNSRNVL PGKVVFTVDI RSPDKAKLDR MRAKIEAQAP KICDTLGVGC
SIEVIGHFAP VTFDEKLVTA VRSAAERLGY THMNLISGAG HDACWAAKVA PATMVMCPCV
DGLSHNEAEE ISKEWATAGA DVLFHAVVET AEIVV
//
