(data stored in ACNUC7421 zone)

SWISSPROT: ALR1_BACSU

ID   ALR1_BACSU              Reviewed;         389 AA.
AC   P10725; P96620;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   11-DEC-2019, entry version 143.
DE   RecName: Full=Alanine racemase 1 {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr1; Synonyms=alr, dal; OrderedLocusNames=BSU04640;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
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 use
RT   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 Bacillus
RT   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   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).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC       also act on other amino acids. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
DR   EMBL; M16207; AAA22378.1; -; Genomic_DNA.
DR   EMBL; AB001488; BAA19301.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12271.1; -; Genomic_DNA.
DR   PIR; JS0443; JS0443.
DR   RefSeq; NP_388345.1; NC_000964.3.
DR   RefSeq; WP_003234284.1; NZ_JNCM01000031.1.
DR   SMR; P10725; -.
DR   STRING; 224308.BSU04640; -.
DR   PaxDb; P10725; -.
DR   PRIDE; P10725; -.
DR   EnsemblBacteria; CAB12271; CAB12271; BSU04640.
DR   GeneID; 939942; -.
DR   KEGG; bsu:BSU04640; -.
DR   PATRIC; fig|224308.179.peg.492; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   InParanoid; P10725; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   PhylomeDB; P10725; -.
DR   BioCyc; BSUB:BSU04640-MONOMER; -.
DR   BRENDA; 5.1.1.1; 658.
DR   SABIO-RK; P10725; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; P10725.
DR   SWISS-2DPAGE; P10725.
KW   Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..389
FT                   /note="Alanine racemase 1"
FT                   /id="PRO_0000114500"
FT   ACT_SITE        41
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   ACT_SITE        266
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         137
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         313
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   MOD_RES         41
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   CONFLICT        40
FT                   /note="V -> E (in Ref. 1; AAA22378)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        66
FT                   /note="V -> M (in Ref. 1; AAA22378)"
FT                   /evidence="ECO:0000305"
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
//

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