ALLC_BACSU
ID ALLC_BACSU Reviewed; 412 AA.
AC O32149;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Allantoate amidohydrolase {ECO:0000303|PubMed:11344136};
DE Short=AAH {ECO:0000250|UniProtKB:P77425};
DE EC=3.5.3.9 {ECO:0000250|UniProtKB:P77425};
DE AltName: Full=Allantoate deiminase {ECO:0000250|UniProtKB:P77425};
GN Name=pucF {ECO:0000303|PubMed:11344136}; Synonyms=yurH;
GN OrderedLocusNames=BSU32530;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION, INDUCTION, AND PATHWAY.
RC STRAIN=168;
RX PubMed=11344136; DOI=10.1128/jb.183.11.3293-3302.2001;
RA Schultz A.C., Nygaard P., Saxild H.H.;
RT "Functional analysis of 14 genes that constitute the purine catabolic
RT pathway in Bacillus subtilis and evidence for a novel regulon controlled by
RT the PucR transcription activator.";
RL J. Bacteriol. 183:3293-3302(2001).
CC -!- FUNCTION: Involved in the anaerobic nitrogen utilization via the
CC assimilation of allantoin (PubMed:11344136). Catalyzes specifically the
CC hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which
CC is unstable and readily undergoes a second deamination by S-
CC ureidoglycine aminohydrolase AllE to yield S-ureidoglycolate and NH3
CC (By similarity). {ECO:0000250|UniProtKB:P77425,
CC ECO:0000269|PubMed:11344136}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=allantoate + 2 H(+) + H2O = (S)-2-ureidoglycine + CO2 +
CC NH4(+); Xref=Rhea:RHEA:27485, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:17536, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:59947; EC=3.5.3.9;
CC Evidence={ECO:0000250|UniProtKB:P77425};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P77425};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P77425};
CC -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation.
CC {ECO:0000305|PubMed:11344136}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P77425}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P77425}.
CC -!- INDUCTION: Transcriptionally regulated by PucR. Expression is very low
CC in excess nitrogen (glutamate plus ammonia) and is induced during
CC limiting-nitrogen conditions (glutamate). Expression is further induced
CC when allantoin is added during limiting-nitrogen conditions.
CC {ECO:0000269|PubMed:11344136}.
CC -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR EMBL; AL009126; CAB15243.1; -; Genomic_DNA.
DR PIR; G70017; G70017.
DR RefSeq; NP_391133.1; NC_000964.3.
DR RefSeq; WP_003228640.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32149; -.
DR SMR; O32149; -.
DR STRING; 224308.BSU32530; -.
DR PaxDb; O32149; -.
DR PRIDE; O32149; -.
DR DNASU; 936699; -.
DR EnsemblBacteria; CAB15243; CAB15243; BSU_32530.
DR GeneID; 936699; -.
DR KEGG; bsu:BSU32530; -.
DR PATRIC; fig|224308.179.peg.3522; -.
DR eggNOG; COG0624; Bacteria.
DR InParanoid; O32149; -.
DR OMA; YWGSGNM; -.
DR PhylomeDB; O32149; -.
DR BioCyc; BSUB:BSU32530-MON; -.
DR UniPathway; UPA00395; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047652; F:allantoate deiminase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0000256; P:allantoin catabolic process; IDA:UniProtKB.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR010158; Amidase_Cbmase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR PANTHER; PTHR32494; PTHR32494; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01879; hydantase; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Metal-binding; Purine metabolism; Reference proteome;
KW Zinc.
FT CHAIN 1..412
FT /note="Allantoate amidohydrolase"
FT /id="PRO_0000061956"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P77425"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P77425"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P77425"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P77425"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P77425"
FT BINDING 218
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000250|UniProtKB:P77425"
FT BINDING 278
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000250|UniProtKB:P77425"
FT BINDING 291
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000250|UniProtKB:P77425"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P77425"
SQ SEQUENCE 412 AA; 45520 MW; 852EC0952E4B5802 CRC64;
MEKQKLSVKN SITDYIEWLA QYGASADGGV TRLLYTKEWM DAQLAVKTEM SSFGLETRFD
DVGNVFGRLS GTQSPDEVIV TGSHIDTVIN GGKYDGAYGV LAAMLALKQL KETYGAPKKT
LEAVSLCEEE GSRFPMTYWG SGNMTGVFSE QDAKEPRDES GVSLQTAMHE SGFGKGVFQS
AYRTDISAFV ELHIEQGKTL EMSGRDLGIV TSIAGQRRYL VTLEGECNHA GTTSMKWRKD
PLAASSRIIH ELLLRSDELP DELRLTCGKI TAEPNVANVI PGRVQFSIDI RHQHQHVLEQ
FHQDMVALIN GICLQKGIRA VIDEYMRIEP VPMDERLKAA AFETALENGF SCEEMVSGAG
HDAQMIGRRY PACMLFVPSR GGVSHSPKEY TSARQLEIGV RALTDLLYKL AY
