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Database: UniProt
Entry: A0A078LX18_9STAP
LinkDB: A0A078LX18_9STAP
Original site: A0A078LX18_9STAP 
ID   A0A078LX18_9STAP        Unreviewed;       407 AA.
AC   A0A078LX18;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:CDZ99713.1};
GN   Name=allC {ECO:0000313|EMBL:CDZ99713.1};
GN   ORFNames=BN1048_00616 {ECO:0000313|EMBL:CDZ99713.1};
OS   Jeotgalicoccus saudimassiliensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Jeotgalicoccus.
OX   NCBI_TaxID=1461582 {ECO:0000313|EMBL:CDZ99713.1, ECO:0000313|Proteomes:UP000044136};
RN   [1] {ECO:0000313|EMBL:CDZ99713.1, ECO:0000313|Proteomes:UP000044136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13MG44_air {ECO:0000313|EMBL:CDZ99713.1,
RC   ECO:0000313|Proteomes:UP000044136};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (JUL-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}.
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DR   EMBL; CCSE01000001; CDZ99713.1; -; Genomic_DNA.
DR   RefSeq; WP_035808327.1; NZ_CCSE01000001.1.
DR   AlphaFoldDB; A0A078LX18; -.
DR   STRING; 1461582.BN1048_00616; -.
DR   MEROPS; M20.976; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_024588_6_0_9; -.
DR   OrthoDB; 9808195at2; -.
DR   Proteomes; UP000044136; Unassembled WGS sequence.
DR   GO; GO:0047652; F:allantoate deiminase activity; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0009442; P:allantoin assimilation pathway; IEA:InterPro.
DR   CDD; cd03884; M20_bAS; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017591; Allantoate_amidohydrolase.
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; TIGR03176; AllC; 1.
DR   NCBIfam; TIGR01879; hydantase; 1.
DR   PANTHER; PTHR32494:SF5; ALLANTOATE AMIDOHYDROLASE; 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:0000313|EMBL:CDZ99713.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000044136};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   DOMAIN          206..309
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
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         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT   BINDING         212
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         272
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         285
FT                   /ligand="allantoate"
FT                   /ligand_id="ChEBI:CHEBI:17536"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT   BINDING         380
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ   SEQUENCE   407 AA;  44696 MW;  12055B4E374AC828 CRC64;
     MDIRETFEKL DKQFTSYGGL EPRGITRLLY SEEWRQAVSA LQDIFKENGL EVSSDAVGNV
     SGRLVGSEFP DETIMSGSHI DTVAEGGHLD GQFGILAALV ATLYLKEKYG QPKRSIEVLS
     IAEEEGSRFP YTFWGVKNFF NLQNNDDVKD IADGDGIKFV DAMRESGFDF KTDDKVRDDI
     KAFVEVHIEQ GQILEKEEKQ IGVVTGIVGQ KRYTINLKGE ANHAGTTPMG YRKDAVVAFT
     EIVQTLVQKA REIGDPLVIT FGSVKPVPGV VNVVPGEVEF SIDTRHIDEA ELNAFAKTVE
     GTINEVSDKY GITADINLWM EQSPALMDES IVKMIEESAE KVAGGSYKVM PSGAGHDAQI
     FSGYMPTGMI FVPSIGGISH NIEEATDVED LVKGIEVLAE TLYKLAY
//
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