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Database: UniProt
Entry: P94494
LinkDB: P94494
Original site: P94494 
ID   ALR2_BACSU              Reviewed;         394 AA.
AC   P94494;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   05-DEC-2018, entry version 130.
DE   RecName: Full=Alanine racemase 2 {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr2; Synonyms=yncD; OrderedLocusNames=BSU17640;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Borchert S., Klein C., Piksa B., Hammelmann M., Entian K.-D.;
RT   "Sequencing of a 26 kb region of the Bacillus subtilis genome
RT   downstream of spoVJ.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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.,
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: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       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-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; U66480; AAB41097.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13648.1; -; Genomic_DNA.
DR   PIR; F69888; F69888.
DR   RefSeq; NP_389646.1; NC_000964.3.
DR   RefSeq; WP_003244881.1; NZ_JNCM01000035.1.
DR   PDB; 5IRP; X-ray; 2.10 A; A/B=1-394.
DR   PDBsum; 5IRP; -.
DR   ProteinModelPortal; P94494; -.
DR   SMR; P94494; -.
DR   STRING; 224308.Bsubs1_010100009706; -.
DR   PaxDb; P94494; -.
DR   PRIDE; P94494; -.
DR   EnsemblBacteria; CAB13648; CAB13648; BSU17640.
DR   GeneID; 939550; -.
DR   KEGG; bsu:BSU17640; -.
DR   PATRIC; fig|224308.179.peg.1915; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   InParanoid; P94494; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   PhylomeDB; P94494; -.
DR   BioCyc; BSUB:BSU17640-MONOMER; -.
DR   BRENDA; 5.1.1.1; 658.
DR   SABIO-RK; P94494; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
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   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Isomerase; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    394       Alanine racemase 2.
FT                                /FTId=PRO_0000114501.
FT   ACT_SITE     39     39       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    272    272       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     139    139       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     320    320       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      39     39       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   STRAND        8     13       {ECO:0000244|PDB:5IRP}.
FT   HELIX        14     27       {ECO:0000244|PDB:5IRP}.
FT   STRAND       33     37       {ECO:0000244|PDB:5IRP}.
FT   HELIX        39     43       {ECO:0000244|PDB:5IRP}.
FT   HELIX        47     56       {ECO:0000244|PDB:5IRP}.
FT   STRAND       61     66       {ECO:0000244|PDB:5IRP}.
FT   HELIX        67     75       {ECO:0000244|PDB:5IRP}.
FT   STRAND       82     84       {ECO:0000244|PDB:5IRP}.
FT   HELIX        90     92       {ECO:0000244|PDB:5IRP}.
FT   HELIX        93     98       {ECO:0000244|PDB:5IRP}.
FT   STRAND      102    105       {ECO:0000244|PDB:5IRP}.
FT   HELIX       108    121       {ECO:0000244|PDB:5IRP}.
FT   STRAND      127    133       {ECO:0000244|PDB:5IRP}.
FT   STRAND      139    142       {ECO:0000244|PDB:5IRP}.
FT   HELIX       145    157       {ECO:0000244|PDB:5IRP}.
FT   STRAND      161    167       {ECO:0000244|PDB:5IRP}.
FT   HELIX       179    197       {ECO:0000244|PDB:5IRP}.
FT   STRAND      204    206       {ECO:0000244|PDB:5IRP}.
FT   HELIX       210    215       {ECO:0000244|PDB:5IRP}.
FT   HELIX       217    219       {ECO:0000244|PDB:5IRP}.
FT   STRAND      223    226       {ECO:0000244|PDB:5IRP}.
FT   HELIX       228    231       {ECO:0000244|PDB:5IRP}.
FT   HELIX       237    241       {ECO:0000244|PDB:5IRP}.
FT   STRAND      251    256       {ECO:0000244|PDB:5IRP}.
FT   STRAND      259    262       {ECO:0000244|PDB:5IRP}.
FT   STRAND      269    271       {ECO:0000244|PDB:5IRP}.
FT   HELIX       272    274       {ECO:0000244|PDB:5IRP}.
FT   STRAND      282    288       {ECO:0000244|PDB:5IRP}.
FT   HELIX       291    293       {ECO:0000244|PDB:5IRP}.
FT   HELIX       297    299       {ECO:0000244|PDB:5IRP}.
FT   TURN        300    302       {ECO:0000244|PDB:5IRP}.
FT   STRAND      304    307       {ECO:0000244|PDB:5IRP}.
FT   STRAND      310    314       {ECO:0000244|PDB:5IRP}.
FT   STRAND      323    329       {ECO:0000244|PDB:5IRP}.
FT   STRAND      338    345       {ECO:0000244|PDB:5IRP}.
FT   STRAND      348    350       {ECO:0000244|PDB:5IRP}.
FT   HELIX       352    358       {ECO:0000244|PDB:5IRP}.
FT   HELIX       363    368       {ECO:0000244|PDB:5IRP}.
FT   STRAND      376    380       {ECO:0000244|PDB:5IRP}.
FT   STRAND      383    385       {ECO:0000244|PDB:5IRP}.
SQ   SEQUENCE   394 AA;  43648 MW;  FE446C21107FBA6E CRC64;
     MIKLCREVWI EVNLDAVKKN LRAIRRHIPH KSKIMAVVKA NGYGHGSIEV ARHALEHGAS
     ELAVASVEEG IVLRKAGITA PILVLGFTSL SCVKKSAAWN ITLSAFQVDW MKEANEILEK
     EASANRLAIH INVDTGMGRL GVRTKEELLE VVKALKASKF LRWTGIFTHF STADEPDTTL
     TKLQHEKFIS FLSFLKKQGI ELPTVHMCNT AAAIAFPEFS ADMIRLGIGL YGLYPSAYIK
     QLNLVKLEPA LSLKARIAYV KTMRTEPRTV SYGATYIAEP NEVIATLPIG YADGYSRALS
     NRGFVLHRGK RVPVAGRVTM DMIMVSLGEN GEGKQGDEVV IYGKQKGAEI SVDEVAEMLN
     TINYEVVSTL SRRIPRFYIR DGEIFKVSTP VLYV
//
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