ID A0A099PCS4_9GAMM Unreviewed; 429 AA.
AC A0A099PCS4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:KGK42743.1};
GN ORFNames=LH51_04875 {ECO:0000313|EMBL:KGK42743.1};
OS Nitrincola sp. A-D6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Nitrincola.
OX NCBI_TaxID=1545442 {ECO:0000313|EMBL:KGK42743.1, ECO:0000313|Proteomes:UP000029924};
RN [1] {ECO:0000313|EMBL:KGK42743.1, ECO:0000313|Proteomes:UP000029924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-D6 {ECO:0000313|EMBL:KGK42743.1,
RC ECO:0000313|Proteomes:UP000029924};
RA Valdes N., Rivera-Araya J., Bijman J., Escudero G L., Demergasso C.,
RA Fernandez S., Ferrer A., Chavez R., Levican G.;
RT "Draft Genome Sequence of the Arsenic-Resistant Bacterium Nitrincola sp.
RT Strain A-D6 Isolated from a Salt Flat in Northern Chile.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGK42743.1}.
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DR EMBL; JRLB01000024; KGK42743.1; -; Genomic_DNA.
DR RefSeq; WP_036520324.1; NZ_JRLB01000024.1.
DR AlphaFoldDB; A0A099PCS4; -.
DR STRING; 1545442.LH51_04875; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000029924; Unassembled WGS sequence.
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 NCBIfam; TIGR01879; hydantase; 1.
DR PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 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:KGK42743.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029924};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 429 AA; 46624 MW; 9848687E5986FD96 CRC64;
MKPVKVNKAR LWDSLMEMAK IGATEKGGCC RLALTDLDRQ ARDLYIRWAE EAGCSIRVDA
VGNIMATRPG EDMSLPPVGT GSHLDTQPTG GKYDGVFGVL SGLEVVRSLN DHGIKTRHPV
EISVWTNEEG SRFAPAMMGS GVVSGRFTLQ EILDKTDVDG IRLGDELERI GYAGDTPVTG
RQYHAFFETH IEQGPYLEAE NKVIGVVTGG QGQRWYDVEL TGQESHAGTT PMHLRTDALT
CASSLILAVQ AIAQQHKPGC GTVGFMQVMP NSRNTIPGKI NLSVDLRHPD DAQLSAMDAE
LTKTVEQLIA DTGVRIELKP IWYYAPIPFD KYCIEAVRDS AADLGYSHMD IIAGAGHDAC
YVSDFAPTSM VFTPCLNGIS HNEIESTTPE ECEAGCSVLL NAMLRMAEVV SADTDLEEET
LVLHRVGEL
//
