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Database: UniProt
Entry: F3KQ91_9BURK
LinkDB: F3KQ91_9BURK
Original site: F3KQ91_9BURK 
ID   F3KQ91_9BURK            Unreviewed;       398 AA.
AC   F3KQ91;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Amidase, hydantoinase/carbamoylase {ECO:0000313|EMBL:EGI78058.1};
GN   ORFNames=HGR_03027 {ECO:0000313|EMBL:EGI78058.1};
OS   Hylemonella gracilis ATCC 19624.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hylemonella.
OX   NCBI_TaxID=887062 {ECO:0000313|EMBL:EGI78058.1, ECO:0000313|Proteomes:UP000016368};
RN   [1] {ECO:0000313|EMBL:EGI78058.1, ECO:0000313|Proteomes:UP000016368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19624 {ECO:0000313|EMBL:EGI78058.1,
RC   ECO:0000313|Proteomes:UP000016368};
RX   PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA   Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA   Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA   Jensen G.J.;
RT   "Structural diversity of bacterial flagellar motors.";
RL   EMBO J. 30:2972-2981(2011).
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:EGI78058.1}.
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DR   EMBL; AEGR01000032; EGI78058.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3KQ91; -.
DR   STRING; 887062.HGR_03027; -.
DR   eggNOG; COG0624; Bacteria.
DR   Proteomes; UP000016368; 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};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016368};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   DOMAIN          201..296
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         371
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ   SEQUENCE   398 AA;  42618 MW;  BCEC423A165569B6 CRC64;
     MDLARIGATP RGGVRRLALT DEDRQGRDQV VRWFREAGLE VRVDEVGNVF GRRAGVDPSA
     PAVATGSHID TQPSGGKFDG NYGVLAGLEV VRTLNDHGLR TRAPLEVVFW TNEEGSRFTP
     VMMGSGAFAG LFTPEFIRER ADIEGKTVGN ELTRIGYRGP QPCGQVPGGG MYAAYFEAHI
     EQGPVLEDAD LPIGIVTGAL GQQWYDVVVT GQDAHAGPTP MALRRDAMLA AARMIDAVNR
     IALAEAPHGR GTVGFIQAEP NSRNVIPGRV RFSVDFRNLT QAGLDRMDAS MREAFAMAAA
     QCQCEVDIAQ VTKFKPCAFH PDCVDSVRDA ARALNLPHMD VVSGAGHDAV YLNAVAPSGM
     IFVPCKDGIS HNEIEDAQPE HLAAGADVLL RAMLAHAS
//
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