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Database: UniProt
Entry: W4LWT6_9BACT
LinkDB: W4LWT6_9BACT
Original site: W4LWT6_9BACT 
ID   W4LWT6_9BACT            Unreviewed;       410 AA.
AC   W4LWT6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:ETX02380.1};
GN   ORFNames=ETSY2_35675 {ECO:0000313|EMBL:ETX02380.1};
OS   Candidatus Entotheonella gemina.
OC   Bacteria; Nitrospinae/Tectomicrobia group; Candidatus Tectomicrobia;
OC   Entotheonella.
OX   NCBI_TaxID=1429439 {ECO:0000313|EMBL:ETX02380.1, ECO:0000313|Proteomes:UP000019140};
RN   [1] {ECO:0000313|EMBL:ETX02380.1, ECO:0000313|Proteomes:UP000019140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSY2 {ECO:0000313|Proteomes:UP000019140};
RX   PubMed=24476823; DOI=10.1038/nature12959;
RA   Wilson M.C., Mori T., Ruckert C., Uria A.R., Helf M.J., Takada K.,
RA   Gernert C., Steffens U.A., Heycke N., Schmitt S., Rinke C., Helfrich E.J.,
RA   Brachmann A.O., Gurgui C., Wakimoto T., Kracht M., Crusemann M.,
RA   Hentschel U., Abe I., Matsunaga S., Kalinowski J., Takeyama H., Piel J.;
RT   "An environmental bacterial taxon with a large and distinct metabolic
RT   repertoire.";
RL   Nature 506:58-62(2014).
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:ETX02380.1}.
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DR   EMBL; AZHX01001536; ETX02380.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4LWT6; -.
DR   PATRIC; fig|1429439.4.peg.6029; -.
DR   HOGENOM; CLU_024588_2_1_7; -.
DR   Proteomes; UP000019140; 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   Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019140};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   DOMAIN          211..312
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         217
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         277
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         290
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         382
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ   SEQUENCE   410 AA;  43929 MW;  B12C26A82420DAB8 CRC64;
     MTLPIDEQRL WNRHMTMAQI GATPKGGVNR QALSPEDVQA RQLLTSWARE LGFTVSTDEI
     GNLFVRREGS ESHAAPVLTG SHLDSQPTGG KFDGAYGVLA GFEALQAIHE TGVATKRPLE
     VVAWVNEEGS RFQPGCTGSL IFSGKARLDD LLAHVDPAGI KFGDALQDSL KALPDIARRS
     TGFDVDTYIE AHIEQGPRLE AEGLPIGIVT GIQGMHRYSV EVVGEEAHAG TAPLKTRKDA
     LKAAAEMVGA LEEVMADDTD TVRFTVGRFE VSPGSPNTVP GRVFFTIDFR HPIQETIDRL
     TARIEPVCRA HARGCQVVVT QISATSPVHF GTNTIDAIRQ QAANLGLPHM DLFSGAGHDA
     GHLASVCPAG MVFVPCEKGI SHNEVENARP ADLAAGAQVL ASFLLERANR
//
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