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Database: UniProt
Entry: P0A2W8
LinkDB: P0A2W8
Original site: P0A2W8 
ID   ALR_STRPN               Reviewed;         367 AA.
AC   P0A2W8; Q54899; Q9S3V7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   05-DEC-2018, entry version 88.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; Synonyms=alaR; OrderedLocusNames=SP_1698;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Guynn L.J., Strych U., Benedik M.J.;
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T.,
RA   Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C.,
RA   Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-367.
RX   PubMed=8830261; DOI=10.1046/j.1365-2958.1996.445975.x;
RA   Martin B., Sharples G.J., Humbert O., Lloyd R.G., Claverys J.-P.;
RT   "The mmsA locus of Streptococcus pneumoniae encodes a RecG-like
RT   protein involved in DNA repair and in three-strand recombination.";
RL   Mol. Microbiol. 19:1035-1045(1996).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL
RP   PHOSPHATE, COFACTOR, SUBUNIT, PYRIDOXAL PHOSPHATE AT LYS-40, AND
RP   CARBAMYLATION AT LYS-129.
RX   PubMed=21612658; DOI=10.1186/1471-2180-11-116;
RA   Im H., Sharpe M.L., Strych U., Davlieva M., Krause K.L.;
RT   "The crystal structure of alanine racemase from Streptococcus
RT   pneumoniae, a target for structure-based drug design.";
RL   BMC Microbiol. 11:116-116(2011).
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         ECO:0000269|PubMed:21612658};
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   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21612658}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; AF171873; AAD51027.1; -; Genomic_DNA.
DR   EMBL; AE005672; AAK75776.1; -; Genomic_DNA.
DR   EMBL; Z49988; CAA90279.1; -; Genomic_DNA.
DR   PIR; G95197; G95197.
DR   PIR; S71015; S71015.
DR   RefSeq; WP_000648075.1; NZ_AKVY01000001.1.
DR   PDB; 3S46; X-ray; 2.00 A; A/B=1-367.
DR   PDBsum; 3S46; -.
DR   ProteinModelPortal; P0A2W8; -.
DR   SMR; P0A2W8; -.
DR   EnsemblBacteria; AAK75776; AAK75776; SP_1698.
DR   KEGG; spn:SP_1698; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   BioCyc; SPNE170187:G1FZB-1721-MONOMER; -.
DR   BRENDA; 5.1.1.1; 1960.
DR   UniPathway; UPA00042; UER00497.
DR   EvolutionaryTrace; P0A2W8; -.
DR   Proteomes; UP000000585; 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.
FT   CHAIN         1    367       Alanine racemase.
FT                                /FTId=PRO_0000114581.
FT   ACT_SITE     40     40       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    263    263       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     136    136       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     310    310       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      40     40       N6-(pyridoxal phosphate)lysine.
FT   MOD_RES     129    129       N6-carboxylysine.
FT                                {ECO:0000269|PubMed:21612658}.
FT   CONFLICT    354    354       V -> E (in Ref. 3; CAA90279).
FT                                {ECO:0000305}.
FT   STRAND       10     14       {ECO:0000244|PDB:3S46}.
FT   HELIX        15     27       {ECO:0000244|PDB:3S46}.
FT   STRAND       34     38       {ECO:0000244|PDB:3S46}.
FT   TURN         42     46       {ECO:0000244|PDB:3S46}.
FT   HELIX        48     55       {ECO:0000244|PDB:3S46}.
FT   HELIX        56     58       {ECO:0000244|PDB:3S46}.
FT   STRAND       60     66       {ECO:0000244|PDB:3S46}.
FT   HELIX        67     75       {ECO:0000244|PDB:3S46}.
FT   STRAND       82     87       {ECO:0000244|PDB:3S46}.
FT   HELIX        90     92       {ECO:0000244|PDB:3S46}.
FT   HELIX        93     98       {ECO:0000244|PDB:3S46}.
FT   STRAND      102    105       {ECO:0000244|PDB:3S46}.
FT   HELIX       108    116       {ECO:0000244|PDB:3S46}.
FT   STRAND      125    130       {ECO:0000244|PDB:3S46}.
FT   STRAND      136    139       {ECO:0000244|PDB:3S46}.
FT   HELIX       142    154       {ECO:0000244|PDB:3S46}.
FT   STRAND      158    164       {ECO:0000244|PDB:3S46}.
FT   HELIX       175    189       {ECO:0000244|PDB:3S46}.
FT   STRAND      196    201       {ECO:0000244|PDB:3S46}.
FT   HELIX       203    208       {ECO:0000244|PDB:3S46}.
FT   HELIX       210    212       {ECO:0000244|PDB:3S46}.
FT   STRAND      215    219       {ECO:0000244|PDB:3S46}.
FT   HELIX       221    224       {ECO:0000244|PDB:3S46}.
FT   TURN        228    231       {ECO:0000244|PDB:3S46}.
FT   STRAND      243    248       {ECO:0000244|PDB:3S46}.
FT   STRAND      250    255       {ECO:0000244|PDB:3S46}.
FT   STRAND      260    262       {ECO:0000244|PDB:3S46}.
FT   HELIX       263    265       {ECO:0000244|PDB:3S46}.
FT   STRAND      273    279       {ECO:0000244|PDB:3S46}.
FT   HELIX       282    284       {ECO:0000244|PDB:3S46}.
FT   HELIX       288    290       {ECO:0000244|PDB:3S46}.
FT   STRAND      294    297       {ECO:0000244|PDB:3S46}.
FT   STRAND      300    304       {ECO:0000244|PDB:3S46}.
FT   STRAND      313    319       {ECO:0000244|PDB:3S46}.
FT   STRAND      326    333       {ECO:0000244|PDB:3S46}.
FT   STRAND      336    338       {ECO:0000244|PDB:3S46}.
FT   HELIX       340    347       {ECO:0000244|PDB:3S46}.
FT   HELIX       351    356       {ECO:0000244|PDB:3S46}.
FT   STRAND      364    367       {ECO:0000244|PDB:3S46}.
SQ   SEQUENCE   367 AA;  39858 MW;  A79E2F1B439B18B7 CRC64;
     MKASPHRPTK ALIHLGAIRQ NIQQMGAHIP QGTLKLAVVK ANAYGHGAVA VAKAIQDDVD
     GFCVSNIDEA IELRQAGLSK PILILGVSEI EAVALAKEYD FTLTVAGLEW IQALLDKEVD
     LTGLTVHLKI DSGMGRIGFR EASEVEQAQD LLQQHGVCVE GIFTHFATAD EESDDYFNAQ
     LERFKTILAS MKEVPELVHA SNSATTLWHV ETIFNAVRMG DAMYGLNPSG AVLDLPYDLI
     PALTLESALV HVKTVPAGAC MGYGATYQAD SEQVIATVPI GYADGWTRDM QNFSVLVDGQ
     ACPIVGRVSM DQITIRLPKL YPLGTKVTLI GSNGDKEITA TQVATYRVTI NYEVVCLLSD
     RIPREYY
//
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