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Database: UniProt
Entry: P0A6B4
LinkDB: P0A6B4
Original site: P0A6B4 
ID   ALR1_ECOLI              Reviewed;         359 AA.
AC   P0A6B4; P29743; P78136; Q2M6Q1;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   13-FEB-2019, entry version 112.
DE   RecName: Full=Alanine racemase, biosynthetic {ECO:0000305|PubMed:18434499};
DE            EC=5.1.1.1 {ECO:0000269|PubMed:18434499};
GN   Name=alr {ECO:0000303|PubMed:18434499, ECO:0000303|PubMed:8335265};
GN   OrderedLocusNames=b4053, JW4013;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8335265; DOI=10.1016/0378-1119(93)90690-5;
RA   Lilley P.E., Stamford N.P., Vasudevan S.G., Dixon N.E.;
RT   "The 92-min region of the Escherichia coli chromosome: location and
RT   cloning of the ubiA and alr genes.";
RL   Gene 129:9-16(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA   Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J.,
RA   Daniels D.L.;
RT   "Analysis of the Escherichia coli genome. IV. DNA sequence of the
RT   region from 89.2 to 92.8 minutes.";
RL   Nucleic Acids Res. 21:5408-5417(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX   PubMed=6323420;
RA   Nakayama N., Arai N., Bond M.W., Kaziro Y., Arai K.;
RT   "Nucleotide sequence of dnaB and the primary structure of the dnaB
RT   protein from Escherichia coli.";
RL   J. Biol. Chem. 259:97-101(1984).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 320-359.
RC   STRAIN=K12;
RX   PubMed=3907634; DOI=10.1016/0006-291X(85)91851-0;
RA   Kuramitsu S., Inoue K., Ogawa T., Ogawa H., Kagamiyama H.;
RT   "Aromatic amino acid aminotransferase of Escherichia coli: nucleotide
RT   sequence of the tyrB gene.";
RL   Biochem. Biophys. Res. Commun. 133:134-139(1985).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEXES WITH D-CYCLOSERINE
RP   AND PYRIDOXAL PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, PYRIDOXAL PHOSPHATE
RP   AT LYS-34, MUTAGENESIS OF ASP-164; GLU-165; PRO-219 AND GLU-221, AND
RP   CARBAMYLATION AT LYS-122.
RX   PubMed=18434499; DOI=10.1110/ps.083495908;
RA   Wu D., Hu T., Zhang L., Chen J., Du J., Ding J., Jiang H., Shen X.;
RT   "Residues Asp164 and Glu165 at the substrate entryway function
RT   potently in substrate orientation of alanine racemase from E. coli:
RT   Enzymatic characterization with crystal structure analysis.";
RL   Protein Sci. 17:1066-1076(2008).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. Provides the D-alanine required for cell wall
CC       biosynthesis. {ECO:0000269|PubMed:18434499}.
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:0000269|PubMed:18434499};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:18434499};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.31 mM for D-alanine {ECO:0000269|PubMed:18434499};
CC         KM=1.00 mM for L-alanine {ECO:0000269|PubMed:18434499};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000269|PubMed:18434499}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000305|PubMed:18434499}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18434499}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; U00006; AAC43147.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77023.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78055.1; -; Genomic_DNA.
DR   EMBL; K01174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M12047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; D65213; PC1296.
DR   RefSeq; NP_418477.1; NC_000913.3.
DR   RefSeq; WP_001147328.1; NZ_LN832404.1.
DR   PDB; 2RJG; X-ray; 2.40 A; A/B/C/D=1-359.
DR   PDB; 2RJH; X-ray; 2.40 A; A/B/C/D=1-359.
DR   PDB; 3B8T; X-ray; 3.00 A; A/B/C/D=1-359.
DR   PDB; 3B8U; X-ray; 3.00 A; A/B/C/D=1-359.
DR   PDB; 3B8V; X-ray; 2.60 A; A/B/C/D=1-359.
DR   PDB; 3B8W; X-ray; 2.70 A; A/B/C/D=1-359.
DR   PDB; 4WR3; X-ray; 1.90 A; A/B/C/D=1-359.
DR   PDB; 4XBJ; X-ray; 2.25 A; A/B/C/D=1-359.
DR   PDBsum; 2RJG; -.
DR   PDBsum; 2RJH; -.
DR   PDBsum; 3B8T; -.
DR   PDBsum; 3B8U; -.
DR   PDBsum; 3B8V; -.
DR   PDBsum; 3B8W; -.
DR   PDBsum; 4WR3; -.
DR   PDBsum; 4XBJ; -.
DR   ProteinModelPortal; P0A6B4; -.
DR   SMR; P0A6B4; -.
DR   BioGrid; 4260823; 598.
DR   IntAct; P0A6B4; 6.
DR   STRING; 316385.ECDH10B_4242; -.
DR   BindingDB; P0A6B4; -.
DR   ChEMBL; CHEMBL2833; -.
DR   PaxDb; P0A6B4; -.
DR   PRIDE; P0A6B4; -.
DR   EnsemblBacteria; AAC77023; AAC77023; b4053.
DR   EnsemblBacteria; BAE78055; BAE78055; BAE78055.
DR   GeneID; 948564; -.
DR   KEGG; ecj:JW4013; -.
DR   KEGG; eco:b4053; -.
DR   PATRIC; fig|1411691.4.peg.2654; -.
DR   EchoBASE; EB0001; -.
DR   EcoGene; EG10001; alr.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   InParanoid; P0A6B4; -.
DR   KO; K01775; -.
DR   PhylomeDB; P0A6B4; -.
DR   BioCyc; EcoCyc:ALARACEBIOSYN-MONOMER; -.
DR   BioCyc; ECOL316407:JW4013-MONOMER; -.
DR   BioCyc; MetaCyc:ALARACEBIOSYN-MONOMER; -.
DR   BRENDA; 5.1.1.1; 2026.
DR   SABIO-RK; P0A6B4; -.
DR   UniPathway; UPA00042; UER00497.
DR   UniPathway; UPA00219; -.
DR   EvolutionaryTrace; P0A6B4; -.
DR   PRO; PR:P0A6B4; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IDA:EcoCyc.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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; Cell shape; Cell wall biogenesis/degradation;
KW   Complete proteome; Isomerase; Peptidoglycan synthesis;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    359       Alanine racemase, biosynthetic.
FT                                /FTId=PRO_0000114514.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    255    255       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     129    129       Substrate. {ECO:0000305|PubMed:18434499}.
FT   BINDING     303    303       Substrate; via amide nitrogen.
FT                                {ECO:0000305|PubMed:18434499}.
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000269|PubMed:18434499}.
FT   MOD_RES     122    122       N6-carboxylysine.
FT                                {ECO:0000269|PubMed:18434499}.
FT   MUTAGEN     164    164       D->A: Slightly reduces affinity for D-Ala
FT                                and L-Ala. {ECO:0000269|PubMed:18434499}.
FT   MUTAGEN     164    164       D->K: Reduces catalytic activity.
FT                                Slightly reduces affinity for D-Ala and
FT                                L-Ala. {ECO:0000269|PubMed:18434499}.
FT   MUTAGEN     165    165       E->A: Slightly reduces affinity for D-Ala
FT                                and L-Ala. {ECO:0000269|PubMed:18434499}.
FT   MUTAGEN     165    165       E->K: Reduces catalytic activity.
FT                                Slightly reduces affinity for D-Ala and
FT                                L-Ala. {ECO:0000269|PubMed:18434499}.
FT   MUTAGEN     219    219       P->A: No effect on catalytic activity. No
FT                                effect on affinity for D-Ala and L-Ala.
FT                                {ECO:0000269|PubMed:18434499}.
FT   MUTAGEN     221    221       E->A,K,P: Slightly increases catalytic
FT                                activity. Slightly increases affinity for
FT                                D-Ala and L-Ala.
FT                                {ECO:0000269|PubMed:18434499}.
FT   STRAND        4      9       {ECO:0000244|PDB:4WR3}.
FT   HELIX        10     23       {ECO:0000244|PDB:4WR3}.
FT   STRAND       27     32       {ECO:0000244|PDB:4WR3}.
FT   HELIX        34     38       {ECO:0000244|PDB:4WR3}.
FT   HELIX        42     48       {ECO:0000244|PDB:4WR3}.
FT   STRAND       53     59       {ECO:0000244|PDB:4WR3}.
FT   HELIX        60     68       {ECO:0000244|PDB:4WR3}.
FT   STRAND       75     77       {ECO:0000244|PDB:4WR3}.
FT   HELIX        84     86       {ECO:0000244|PDB:4WR3}.
FT   HELIX        87     92       {ECO:0000244|PDB:4WR3}.
FT   STRAND       95     99       {ECO:0000244|PDB:4WR3}.
FT   HELIX       102    110       {ECO:0000244|PDB:4WR3}.
FT   STRAND      119    123       {ECO:0000244|PDB:4WR3}.
FT   STRAND      125    127       {ECO:0000244|PDB:4XBJ}.
FT   STRAND      129    132       {ECO:0000244|PDB:4WR3}.
FT   HELIX       134    145       {ECO:0000244|PDB:4WR3}.
FT   STRAND      148    150       {ECO:0000244|PDB:2RJG}.
FT   STRAND      155    157       {ECO:0000244|PDB:4WR3}.
FT   HELIX       170    182       {ECO:0000244|PDB:4WR3}.
FT   HELIX       194    199       {ECO:0000244|PDB:4WR3}.
FT   HELIX       201    203       {ECO:0000244|PDB:4WR3}.
FT   STRAND      205    208       {ECO:0000244|PDB:4WR3}.
FT   HELIX       212    215       {ECO:0000244|PDB:4WR3}.
FT   STRAND      221    223       {ECO:0000244|PDB:4WR3}.
FT   HELIX       226    229       {ECO:0000244|PDB:4WR3}.
FT   STRAND      235    247       {ECO:0000244|PDB:4WR3}.
FT   STRAND      252    254       {ECO:0000244|PDB:4WR3}.
FT   HELIX       255    257       {ECO:0000244|PDB:4WR3}.
FT   STRAND      265    271       {ECO:0000244|PDB:4WR3}.
FT   TURN        274    277       {ECO:0000244|PDB:4WR3}.
FT   STRAND      287    290       {ECO:0000244|PDB:4WR3}.
FT   STRAND      293    297       {ECO:0000244|PDB:4WR3}.
FT   STRAND      303    309       {ECO:0000244|PDB:4WR3}.
FT   STRAND      321    326       {ECO:0000244|PDB:4WR3}.
FT   HELIX       331    338       {ECO:0000244|PDB:4WR3}.
FT   HELIX       342    347       {ECO:0000244|PDB:4WR3}.
FT   STRAND      353    358       {ECO:0000244|PDB:4WR3}.
SQ   SEQUENCE   359 AA;  39153 MW;  FDE9B438115342C2 CRC64;
     MQAATVVINR RALRHNLQRL RELAPASKMV AVVKANAYGH GLLETARTLP DADAFGVARL
     EEALRLRAGG ITKPVLLLEG FFDARDLPTI SAQHFHTAVH NEEQLAALEE ASLDEPVTVW
     MKLDTGMHRL GVRPEQAEAF YHRLTQCKNV RQPVNIVSHF ARADEPKCGA TEKQLAIFNT
     FCEGKPGQRS IAASGGILLW PQSHFDWVRP GIILYGVSPL EDRSTGADFG CQPVMSLTSS
     LIAVREHKAG EPVGYGGTWV SERDTRLGVV AMGYGDGYPR AAPSGTPVLV NGREVPIVGR
     VAMDMICVDL GPQAQDKAGD PVILWGEGLP VERIAEMTKV SAYELITRLT SRVAMKYVD
//
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