ALLB_ALKHC
ID ALLB_ALKHC Reviewed; 438 AA.
AC Q9KAH8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
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}; OrderedLocusNames=BH2309;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
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;
CC Evidence={ECO:0000255|HAMAP-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; 272558.10174929; -.
DR PRIDE; Q9KAH8; -.
DR DNASU; 892154; -.
DR EnsemblBacteria; BAB06028; BAB06028; BAB06028.
DR KEGG; bha:BH2309; -.
DR eggNOG; COG0044; Bacteria.
DR HOGENOM; CLU_015572_4_2_9; -.
DR OMA; WVTAEVT; -.
DR OrthoDB; 906155at2; -.
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; 2.30.40.10; -; 2.
DR HAMAP; MF_01645; Hydantoinase; 1.
DR InterPro; IPR017593; Allantoinase.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR03178; allantoinase; 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
