ID ALR1_BACSU STANDARD; PRT; 389 AA. AC P10725; P96620; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 21-MAR-2006, entry version 57. DE Alanine racemase 1 (EC 5.1.1.1). GN Name=alr1; Synonyms=alr, dal; OrderedLocusNames=BSU04640; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Ferrari E., Henner D.J., Yang M.Y.; RT "Isolation of an alanine racemase gene from Bacillus subtilis and its RT use for plasmid maintenance in B. subtilis."; RL Biotechnology (N.Y.) 3:1003-1007(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RA Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.; RT "A 148 kbp sequence of the region between 35 and 47 degree of the RT Bacillus subtilis genome."; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [3] 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). CC -!- FUNCTION: Provides the D-alanine required for cell wall CC biosynthesis. CC -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. CC -!- COFACTOR: Pyridoxal phosphate. CC -!- PATHWAY: D-alanine branch of peptidoglycan biosynthesis; first CC step. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the alanine racemase 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; M16207; AAA22378.1; -; Genomic_DNA. DR EMBL; AB001488; BAA19301.1; -; Genomic_DNA. DR EMBL; Z99106; CAB12271.1; -; Genomic_DNA. DR PIR; JS0443; JS0443. DR HSSP; P10724; 1L6G. DR SubtiList; BG10950; alr1. DR GenomeReviews; AL009126_GR; BSU04640. DR BioCyc; BSUB1423:BSU0464-MONOMER; -. DR HAMAP; MF_01201; -; 1. DR InterPro; IPR012155; Ala_racemase. DR InterPro; IPR011079; Ala_racemase_C. DR InterPro; IPR001608; Ala_racemase_N. DR InterPro; IPR000821; Ala_racemase_reg. DR InterPro; IPR009006; Racem_decarbox_C. DR Pfam; PF00842; Ala_racemase_C; 1. DR Pfam; PF01168; Ala_racemase_N; 1. DR PIRSF; PIRSF001401; Ala_racemase; 1. DR PRINTS; PR00992; ALARACEMASE. DR TIGRFAMs; TIGR00492; alr; 1. DR PROSITE; PS00395; ALANINE_RACEMASE; 1. KW Cell shape; Cell wall; Complete proteome; Isomerase; KW Peptidoglycan synthesis; Pyridoxal phosphate. FT CHAIN 1 389 Alanine racemase 1. FT /FTId=PRO_0000114500. FT ACT_SITE 41 41 Proton acceptor; specific for D-alanine FT (By similarity). FT ACT_SITE 266 266 Proton acceptor; specific for L-alanine FT (By similarity). FT BINDING 41 41 Pyridoxal phosphate (covalent) (By FT similarity). FT CONFLICT 40 40 V -> E (in Ref. 1). FT CONFLICT 66 66 V -> M (in Ref. 1). SQ SEQUENCE 389 AA; 43265 MW; 4802B7C182ACCD58 CRC64; MSTKPFYRDT WAEIDLSAIK ENVSNMKKHI GEHVHLMAVV KANAYGHGDA ETAKAALDAG ASCLAVAILD EAISLRKKGL KAPILVLGAV PPEYVAIAAE YDVTLTGYSV EWLQEAARHT KKGSLHFHLK VDTGMNRLGV KTEEEVQNVM AILDRNPRLK CKGVFTHFAT ADEKERGYFL MQFERFKELI APLPLKNLMV HCANSAAGLR LKKGFFNAVR FGIGMYGLRP SADMSDEIPF QLRPAFTLHS TLSHVKLIRK GESVSYGAEY TAEKDTWIGT VPVGYADGWL RKLKGTDILV KGKRLKIAGR ICMDQFMVEL DQEYPPGTKV TLIGRQGDEY ISMDEIAGRL ETINYEVACT ISSRVPRMFL ENGSIMEVRN PLLQVNISN //