ID A0A1T1ASX8_RHOFE Unreviewed; 418 AA.
AC A0A1T1ASX8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Zn-dependent hydrolase {ECO:0000313|EMBL:OOV07212.1};
GN ORFNames=RF819_11145 {ECO:0000313|EMBL:OOV07212.1};
OS Rhodoferax fermentans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=28066 {ECO:0000313|EMBL:OOV07212.1, ECO:0000313|Proteomes:UP000190750};
RN [1] {ECO:0000313|EMBL:OOV07212.1, ECO:0000313|Proteomes:UP000190750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 7819 {ECO:0000313|EMBL:OOV07212.1,
RC ECO:0000313|Proteomes:UP000190750};
RA Kim Y.J., Farh M.E.-A., Yang D.-C.;
RT "Genome sequencing of Rhodoferax fermentans JCM 7819.";
RL Submitted (JAN-2017) 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:OOV07212.1}.
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DR EMBL; MTJN01000002; OOV07212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T1ASX8; -.
DR STRING; 28066.RF819_11145; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000190750; 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 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:OOV07212.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000190750};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 219..314
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 418 AA; 44833 MW; 07087D257600DB7D CRC64;
MTTTQTDIST LRINGQRLWD SLMELAQIGA TPKGGVCRLT LTDLDKQGRD LVTKWAREAG
LTVTIDKIGN GFMCRPGRNN ALPPIVTGSH IDTQPTGGKF DGNYGVLAGL EVMRTLNDHG
IETEAPMEVS FWTNEEGSRF VPVMMGSGVF SKTFTLEHAY AAKDIDGKTV GEELARIGYI
GEQEPGDHPI GAFFETHIEQ GPVLEDNDVT IGVVQGVLGI RWFDCTVTGM EAHAGPTPMA
LRKDAMQVAA QIMQEVVATA LRHQPHGRGT VGMVQVFPNS RNVIPGRVKF SIDLRNSTDA
LVDQMADEVK AFAASMSQQT GLGVQIELVS SYPAQAFHED CKGAVAKAAT KLGYSNMPVV
SGAGHDAVYM SQLAPTGMIF IPCKDGISHN EIESATPEHI TAGCNVLLHA MLERAGVA
//
