ID   ALLB_HALH5              Reviewed;         438 AA.
AC   Q9KAH8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Allantoinase {ECO:0000255|HAMAP-Rule:MF_01645};
DE            EC=3.5.2.5 {ECO:0000255|HAMAP-Rule:MF_01645};
DE   AltName: Full=Allantoin-utilizing enzyme {ECO:0000255|HAMAP-Rule:MF_01645};
GN   Name=allB {ECO:0000255|HAMAP-Rule:MF_01645};
GN   Synonyms=pucH {ECO:0000255|HAMAP-Rule:MF_01645};
GN   OrderedLocusNames=BH2309;
OS   Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Halalkalibacterium (ex Joshi et al. 2022).
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
CC   -!- FUNCTION: Catalyzes the conversion of allantoin (5-ureidohydantoin) to
CC       allantoic acid by hydrolytic cleavage of the five-member hydantoin
CC       ring. {ECO:0000255|HAMAP-Rule:MF_01645}.
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:0000255|HAMAP-
CC         Rule:MF_01645};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01645};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01645};
CC   -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation; allantoate
CC       from (S)-allantoin: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01645}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01645}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two zinc ions.
CC       {ECO:0000255|HAMAP-Rule:MF_01645}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Allantoinase family. {ECO:0000255|HAMAP-Rule:MF_01645}.
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DR   EMBL; BA000004; BAB06028.1; -; Genomic_DNA.
DR   PIR; E83938; E83938.
DR   RefSeq; WP_010898465.1; NC_002570.2.
DR   PDB; 3HM7; X-ray; 2.60 A; A/B/C/D/E/F=2-438.
DR   PDBsum; 3HM7; -.
DR   AlphaFoldDB; Q9KAH8; -.
DR   SMR; Q9KAH8; -.
DR   STRING; 272558.gene:10728207; -.
DR   DNASU; 892154; -.
DR   KEGG; bha:BH2309; -.
DR   eggNOG; COG0044; Bacteria.
DR   HOGENOM; CLU_015572_4_2_9; -.
DR   OrthoDB; 9765462at2; -.
DR   UniPathway; UPA00395; UER00653.
DR   EvolutionaryTrace; Q9KAH8; -.
DR   Proteomes; UP000001258; 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; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 2.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Metal-binding; Purine metabolism;
KW   Reference proteome; Zinc.
FT   CHAIN           1..438
FT                   /note="Allantoinase"
FT                   /id="PRO_0000317670"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01645"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   BINDING         242
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   MOD_RES         150
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01645"
FT   STRAND          5..14
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          19..27
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          30..36
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          54..57
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   TURN            68..70
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           72..74
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           78..85
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   TURN            86..88
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          89..94
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          96..101
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           106..113
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           115..119
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          121..129
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           135..137
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           138..143
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          147..155
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           166..179
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          183..186
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           190..202
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           208..214
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           217..234
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          238..240
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           246..257
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          262..266
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           268..272
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           275..281
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           294..306
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           321..324
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   TURN            329..331
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   TURN            339..341
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           342..349
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   TURN            350..354
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           358..365
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           367..373
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   TURN            376..378
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          390..400
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   HELIX           403..405
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          408..410
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   TURN            414..417
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          419..429
FT                   /evidence="ECO:0007829|PDB:3HM7"
FT   STRAND          432..436
FT                   /evidence="ECO:0007829|PDB:3HM7"
SQ   SEQUENCE   438 AA;  48542 MW;  47A24DD790AF947F CRC64;
     MKRFDLIIRS STVVTETTTY RADVAIRNGI VSAITEPGSI SSDDGPAIDG TGLHLFPGMV
     DVHVHFNEPG RTEWEGFASG SKSLAAGGVT TYFDMPLNSN PPTITREELD KKRQLANEKS
     LVDYRFWGGL VPGNIDHLQD LHDGGVIGFK AFMSECGTDD FQFSHDETLL KGMKKIAALG
     SILAVHAESN EMVNALTTIA IEEQRLTVKD YSEARPIVSE LEAVERILRF AQLTCCPIHI
     CHVSSRKVLK RIKQAKGEGV NVSVETCPHY LLFSLDEFAE IGYLAKCAPP LRERQEVEDL
     WDGLMAGEID LISSDHSPSL PQMKTGKTIF EVWGGIAGCQ NTLAVMLTEG YHKRKMPLTQ
     IVQLLSTEPA KRFGLYPQKG TIQVGAEASF TLIDLNESYT LNASDLYYRH PISPYVGQRF
     RGKVKHTICQ GKHVYQDH
//