ID ALN_BACSU STANDARD; PRT; 446 AA. AC O32137; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 21-MAR-2006, entry version 45. DE Allantoinase (EC 3.5.2.5). GN Name=pucH; OrderedLocusNames=BSU32410; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA 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., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA 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. RC STRAIN=168; RX MEDLINE=21242727; PubMed=11344136; RX 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 RT controlled by the PucR transcription activator."; RL J. Bacteriol. 183:3293-3302(2001). CC -!- CATALYTIC ACTIVITY: (S)-allantoin + H(2)O = allantoate. CC -!- COFACTOR: Zinc (By similarity). CC -!- PATHWAY: Degradation of allantoin (purine catabolism); first step. CC -!- INDUCTION: Expression is very low in excess nitrogen (glutamate CC plus ammonia) and is induced during limiting-nitrogen conditions CC (glutamate). Expression is further induced when allantoin or CC allantoate are added during limiting-nitrogen conditions. CC -!- SIMILARITY: Belongs to the DHOase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z99120; CAB15231.1; -; Genomic_DNA. DR PIR; C70016; C70016. DR HSSP; P81006; 1GKR. DR SubtiList; BG13982; pucH. DR GenomeReviews; AL009126_GR; BSU32410. DR BioCyc; BSUB1423:BSU3238-MONOMER; -. DR InterPro; IPR006680; Amidohydro_1. DR InterPro; IPR011059; Metalo_hydrolase. DR Pfam; PF01979; Amidohydro_1; 1. KW Complete proteome; Hydrolase; Metal-binding; Purine metabolism; Zinc. FT CHAIN 1 446 Allantoinase. FT /FTId=PRO_0000165940. FT METAL 60 60 Zinc (Potential). FT METAL 62 62 Zinc (Potential). SQ SEQUENCE 446 AA; 48331 MW; 48515B6414A5C234 CRC64; MAYDMVIKGA KAVTPDGVIE ADIVVQNGVI AEIGSDIEAS GTEIIQADGK YVFPGVIDCH VHFNEPGRED WEGFETGSQM MAAGGCTTYF DMPLNCIPST VTAEHLLAKA ELGRQKSAVD FALWGGLVPG HIEDIRPMAE AGAIGFKAFL SKSGTDEFRS VDERTLLKGM AEIAAAGKIL ALHAESDAIT SYLQMVLANK GKVDADAYAA SRPEEAEVEA VYRTIQYAKV TGCPVHFVHI STAKAVRLIR EAKQEGLDVS VETCPHYVLF SHDDLRQRGS VAKCAPPLRS RQSKETLIET LIAGDIDMVS SDHSPCRPSL KREDNMFLSW GGISGGQFTL LGMLELALEH QIPFETIAEW TAAAPAKRFG LQKKGRLEAG CDADFVLVSM EPYTVTRESM FAKHKKSIYE GHTFPCSISA TYSKGRCVYN DGEKVTEIDG ALVVPS //