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Database: UniProt
Entry: A0A0M3R9Y8_9BACI
LinkDB: A0A0M3R9Y8_9BACI
Original site: A0A0M3R9Y8_9BACI 
ID   A0A0M3R9Y8_9BACI        Unreviewed;       436 AA.
AC   A0A0M3R9Y8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   08-MAY-2019, entry version 22.
DE   RecName: Full=Allantoinase {ECO:0000256|HAMAP-Rule:MF_01645};
DE            EC=3.5.2.5 {ECO:0000256|HAMAP-Rule:MF_01645};
DE   AltName: Full=Allantoin-utilizing enzyme {ECO:0000256|HAMAP-Rule:MF_01645};
GN   Name=allB {ECO:0000256|HAMAP-Rule:MF_01645};
GN   Synonyms=pucH {ECO:0000256|HAMAP-Rule:MF_01645};
GN   ORFNames=AM592_12235 {ECO:0000313|EMBL:ALC82262.1};
OS   Bacillus gobiensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1441095 {ECO:0000313|EMBL:ALC82262.1, ECO:0000313|Proteomes:UP000067625};
RN   [1] {ECO:0000313|Proteomes:UP000067625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-4402 {ECO:0000313|Proteomes:UP000067625};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J.,
RA   Ge C., Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALC82262.1, ECO:0000313|Proteomes:UP000067625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-4402 {ECO:0000313|EMBL:ALC82262.1,
RC   ECO:0000313|Proteomes:UP000067625};
RX   PubMed=26530456; DOI=10.1099/ijsem.0.000729;
RA   Liu B., Liu G.H., Cetin S., Schumann P., Pan Z.Z., Chen Q.Q.;
RT   "Bacillus gobiensis sp. nov., isolated from a soil sample.";
RL   Int. J. Syst. Evol. Microbiol. 66:379-384(2016).
CC   -!- FUNCTION: Catalyzes the conversion of allantoin (5-
CC       ureidohydantoin) to allantoic acid by hydrolytic cleavage of the
CC       five-member hydantoin ring. {ECO:0000256|HAMAP-Rule:MF_01645}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-allantoin + H2O = allantoate + H(+);
CC         Xref=Rhea:RHEA:17029, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15678, ChEBI:CHEBI:17536; EC=3.5.2.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01645};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01645};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01645};
CC   -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation;
CC       allantoate from (S)-allantoin: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01645}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01645}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|PIRSR:PIRSR611612-50}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two zinc
CC       ions. {ECO:0000256|HAMAP-Rule:MF_01645}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Allantoinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01645}.
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DR   EMBL; CP012600; ALC82262.1; -; Genomic_DNA.
DR   RefSeq; WP_053604047.1; NZ_CP012600.1.
DR   EnsemblBacteria; ALC82262; ALC82262; AM592_12235.
DR   PATRIC; fig|1441095.3.peg.2683; -.
DR   OrthoDB; 906155at2; -.
DR   UniPathway; UPA00395; UER00653.
DR   Proteomes; UP000067625; Chromosome.
DR   GO; GO:0004038; F:allantoinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000256; P:allantoin catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_01645; Hydantoinase; 1.
DR   InterPro; IPR017593; Allantoinase.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR03178; allantoinase; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000067625};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01645,
KW   ECO:0000256|SAAS:SAAS00321417, ECO:0000313|EMBL:ALC82262.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01645,
KW   ECO:0000256|SAAS:SAAS00321440};
KW   Purine metabolism {ECO:0000256|HAMAP-Rule:MF_01645};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067625};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01645}.
FT   DOMAIN        4     41       Urease_alpha. {ECO:0000259|Pfam:PF00449}.
FT   DOMAIN       52    431       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   METAL        61     61       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01645}.
FT   METAL        63     63       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01645}.
FT   METAL       148    148       Zinc 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01645}.
FT   METAL       148    148       Zinc 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01645}.
FT   METAL       184    184       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01645}.
FT   METAL       240    240       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01645}.
FT   METAL       313    313       Zinc 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01645}.
FT   MOD_RES     148    148       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01645, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   436 AA;  47626 MW;  3DCAF333CDCD172B CRC64;
     MKPYDLIIKG AQIVAQDGVI SADVGINDGV IAEIGSLSEE DSLDVFKAEG FYVFPGAVDC
     HVHLDEPGRE HWEGFETGTA MLAAGGCTTF FDMPLNGIPS TTSVQAYEEK KKIANEKSVV
     DFALWGGLVP GNFEEIAGLA EAGVIGFKAF LSESGNKEFE AVDDETLLLG MMEIAKHNKI
     LALHSESNVI TRVMQSIFEK KGDVSADAYA ASRPVEAEVE AVERAIQFAK LSGCLLHFVH
     ISSGRAVEAI TRAKEEGMDV TLETCPHYLL FTHDDLKTIG SRAKCAPPLR EKPVRDELVS
     ALIEGKIDMI SSDHSPCPPE MKNEENMFQS WGGISGGQYT LLSVIEVALK YNIPLEKVAY
     WTAESPADRF GLGKKKGKIK AGYDADLTIV DLNQQFTVAK KNMYAKHKVS LYEDHSFPCK
     INATFTRGKL VYSDLT
//
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