ID A0A2W1LBI4_9BACL Unreviewed; 463 AA.
AC A0A2W1LBI4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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 ECO:0000313|EMBL:PZD96099.1};
GN ORFNames=DNH61_09290 {ECO:0000313|EMBL:PZD96099.1};
OS Paenibacillus sambharensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1803190 {ECO:0000313|EMBL:PZD96099.1, ECO:0000313|Proteomes:UP000249522};
RN [1] {ECO:0000313|EMBL:PZD96099.1, ECO:0000313|Proteomes:UP000249522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMB1 {ECO:0000313|EMBL:PZD96099.1,
RC ECO:0000313|Proteomes:UP000249522};
RA Pinnaka A.K., Singh H., Kaur M.;
RT "Paenibacillus imtechensis sp. nov.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of allantoin (5-ureidohydantoin) to
CC allantoic acid by hydrolytic cleavage of the five-member hydantoin
CC ring. {ECO:0000256|HAMAP-Rule:MF_01645}.
CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC to dihydroorotate. {ECO:0000256|ARBA:ARBA00002368}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-allantoin + H2O = allantoate + H(+); Xref=Rhea:RHEA:17029,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15678,
CC ChEBI:CHEBI:17536; EC=3.5.2.5; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01645};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-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; allantoate
CC from (S)-allantoin: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01645}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|HAMAP-Rule:MF_01645}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
CC {ECO:0000256|HAMAP-Rule:MF_01645}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Allantoinase family. {ECO:0000256|HAMAP-Rule:MF_01645}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class I DHOase subfamily.
CC {ECO:0000256|ARBA:ARBA00010286}.
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:PZD96099.1}.
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DR EMBL; QKRB01000042; PZD96099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1LBI4; -.
DR OrthoDB; 9765462at2; -.
DR UniPathway; UPA00395; UER00653.
DR Proteomes; UP000249522; Unassembled WGS sequence.
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; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR HAMAP; MF_01645; Hydantoinase; 1.
DR InterPro; IPR017593; Allantoinase.
DR InterPro; IPR047604; Allantoinase_bact.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR03178; allantoinase; 1.
DR PANTHER; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF4; ALLANTOINASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00482; DIHYDROOROTASE_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01645};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01645};
KW Purine metabolism {ECO:0000256|ARBA:ARBA00022631, ECO:0000256|HAMAP-
KW Rule:MF_01645}; Reference proteome {ECO:0000313|Proteomes:UP000249522};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01645}.
FT DOMAIN 55..436
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01645"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01645"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01645"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01645"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01645"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01645"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01645"
FT MOD_RES 150
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01645"
SQ SEQUENCE 463 AA; 49147 MW; 869D045EC2FC4B0E CRC64;
MSLDLVIHGG SVVLPNRVMP LDIAIRDGRI TALSSRGESE GWPAERRVDA SGLHVFPGMI
DVHVHFNEPN LGHWEGFAAG SAALAAGGCT TYIDMPLNGN PPTVTVKAFE AKLKLASGQS
AVDYCLWGGL VPGNAGELEG MARAGAAGFK AFLSDPGGVG EGRFRQADDW TLYEGMKRIA
SFGGLLALHA ENDTITSMLG EAAAAEGRTD ASSFAASRPV AAETEAVGKA LHFAALTGCR
LHFVHISSPD AVRMITDAKA AGLDVTAETC PHYLLLTDED MAAIGPAAKC APPLRGREQI
EQLWALLEEG QIDLIASDHS PCPTSMKEPA SGSFLDAWGG ISGAQSSLEL MLDEGVKRRG
LSCERISKLL SGNPARRFGL YPNKGEIMVG AEADLALVDM NRSYTLQAEH LKYRHKHSPY
IGRTIGCRVA ATYVRGVKVY DLACREAVAK DHGRPVLPRG IPL
//
