ID J7TGG1_MORMO Unreviewed; 419 AA.
AC J7TGG1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Beta-ureidopropionase {ECO:0000313|EMBL:AGG29146.1};
GN ORFNames=MU9_100 {ECO:0000313|EMBL:AGG29146.1};
OS Morganella morganii subsp. morganii KT.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Morganella.
OX NCBI_TaxID=1124991 {ECO:0000313|EMBL:AGG29146.1, ECO:0000313|Proteomes:UP000011834};
RN [1] {ECO:0000313|EMBL:AGG29146.1, ECO:0000313|Proteomes:UP000011834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT {ECO:0000313|EMBL:AGG29146.1,
RC ECO:0000313|Proteomes:UP000011834};
RX PubMed=23282187;
RA Chen Y.T., Peng H.L., Shia W.C., Hsu F.R., Ken C.F., Tsao Y.M., Chen C.H.,
RA Liu C.E., Hsieh M.F., Chen H.C., Tang C.Y., Ku T.H.;
RT "Whole-genome sequencing and identification of Morganella morganii KT
RT pathogenicity-related genes.";
RL BMC Genomics 13:S4-S4(2012).
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; CP004345; AGG29146.1; -; Genomic_DNA.
DR RefSeq; WP_004234678.1; NC_020418.1.
DR AlphaFoldDB; J7TGG1; -.
DR GeneID; 69677327; -.
DR KEGG; mmk:MU9_100; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_024588_2_1_6; -.
DR Proteomes; UP000011834; Chromosome.
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 GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011834};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 217..315
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 419 AA; 44508 MW; BC29DC65EC314BA8 CRC64;
MNHKSGGLKI DGKTLLNHLQ ELGNAGADPV KGGRTRTALT DAEKQGRDLV VSWMKALDLV
IRIDQIGNIF GTLPSVSGNS DTAPLMIGSH IDTVINAGAL DGCYGVLSGL AVVRAFREAG
VLPSRPITVA AFTNEEGVRF HPDMMGSLVY AGGYPLEDAL NAVATDGAVL RDELERAGYA
GSMVPGSIVP HEYLELHIEQ GPVLEAEGLQ IGVVESLQGI SWQKITITGT ANHAGTTPTR
LRHDAGYAAA KLITFLREGI SQKNGATLTT VGTIAFEPNA VNVIPGSATF TIDMRDPDEE
RLQWAEGQIR DYLAVLSEQE GVTVSARQLA RFQPVVFDKT LVSCVENAAR AAGSAYRRMP
SGAGHDAQMI ARIAPAAMIF VPSKNGISHN PAEYTEDADL IRGAQVLLDT VILRLAEPV
//
