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Database: UniProt
Entry: I6LNY0
LinkDB: I6LNY0
Original site: I6LNY0 
ID   ALR_PSEPU               Reviewed;         409 AA.
AC   I6LNY0;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   05-DEC-2018, entry version 28.
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;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=YZ-26;
RX   PubMed=22806802; DOI=10.1007/s11274-011-0816-1;
RA   Liu J.L., Liu X.Q., Shi Y.W.;
RT   "Expression, purification, and characterization of alanine racemase
RT   from Pseudomonas putida YZ-26.";
RL   World J. Microbiol. Biotechnol. 28:267-274(2012).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. Can also use isoleucine. {ECO:0000269|PubMed:22806802}.
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         ECO:0000269|PubMed:22806802};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- ACTIVITY REGULATION: Activity is enhanced by Co(2+), Mn(2+) and
CC       Sr(2+), and decreased by Cu(2+). {ECO:0000269|PubMed:22806802}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=10.34 mM for L-alanine {ECO:0000269|PubMed:22806802};
CC         Vmax=18.73 mmol/min/mg enzyme {ECO:0000269|PubMed:22806802};
CC       pH dependence:
CC         Optimum pH is 9.0. {ECO:0000269|PubMed:22806802};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.
CC         {ECO:0000269|PubMed:22806802};
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: Monomer. {ECO:0000269|PubMed:22806802}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; GU462155; ADW54426.1; -; Genomic_DNA.
DR   PDB; 4DYJ; X-ray; 2.45 A; A/B=1-409.
DR   PDB; 4FS9; X-ray; 3.10 A; A/B=1-409.
DR   PDBsum; 4DYJ; -.
DR   PDBsum; 4FS9; -.
DR   ProteinModelPortal; I6LNY0; -.
DR   SMR; I6LNY0; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   UniPathway; UPA00042; UER00497.
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; Isomerase; Pyridoxal phosphate.
FT   CHAIN         1    409       Alanine racemase.
FT                                /FTId=PRO_0000422273.
FT   ACT_SITE     75     75       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    301    301       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     174    174       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     349    349       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      75     75       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   STRAND       28     31       {ECO:0000244|PDB:4FS9}.
FT   HELIX        39     41       {ECO:0000244|PDB:4DYJ}.
FT   STRAND       43     49       {ECO:0000244|PDB:4DYJ}.
FT   HELIX        50     64       {ECO:0000244|PDB:4DYJ}.
FT   STRAND       67     73       {ECO:0000244|PDB:4DYJ}.
FT   HELIX        78     80       {ECO:0000244|PDB:4DYJ}.
FT   HELIX        83     92       {ECO:0000244|PDB:4DYJ}.
FT   STRAND       97    102       {ECO:0000244|PDB:4DYJ}.
FT   HELIX       103    111       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      116    122       {ECO:0000244|PDB:4DYJ}.
FT   HELIX       126    131       {ECO:0000244|PDB:4DYJ}.
FT   HELIX       132    135       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      138    141       {ECO:0000244|PDB:4DYJ}.
FT   HELIX       144    156       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      161    167       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      174    177       {ECO:0000244|PDB:4DYJ}.
FT   HELIX       182    192       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      197    203       {ECO:0000244|PDB:4DYJ}.
FT   HELIX       211    231       {ECO:0000244|PDB:4DYJ}.
FT   HELIX       236    238       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      240    242       {ECO:0000244|PDB:4DYJ}.
FT   HELIX       246    251       {ECO:0000244|PDB:4DYJ}.
FT   HELIX       253    256       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      258    263       {ECO:0000244|PDB:4DYJ}.
FT   HELIX       264    266       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      281    293       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      298    300       {ECO:0000244|PDB:4FS9}.
FT   HELIX       301    303       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      308    317       {ECO:0000244|PDB:4DYJ}.
FT   HELIX       320    322       {ECO:0000244|PDB:4DYJ}.
FT   HELIX       326    328       {ECO:0000244|PDB:4DYJ}.
FT   TURN        329    331       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      333    336       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      339    343       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      352    355       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      367    374       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      377    379       {ECO:0000244|PDB:4DYJ}.
FT   HELIX       381    388       {ECO:0000244|PDB:4DYJ}.
FT   HELIX       393    402       {ECO:0000244|PDB:4DYJ}.
FT   STRAND      405    408       {ECO:0000244|PDB:4DYJ}.
SQ   SEQUENCE   409 AA;  44217 MW;  03D668FBAD9C87E7 CRC64;
     MPFRRTLLAA SLVLLITGQA PLYAAPPLSM DNGTNALTVQ NSNAWVEVSA SALQHNIRTL
     QAELAGKSRL CAVLKADAYG HGIGLVMPSI IAQGVPCVAV ASNEEARVVR ASGFTGQLVR
     VRAASLSELE DALQYDMEEL VGSAEFARQA DAIAARHGKT LRIHLAFNSS GMSRNGVEMA
     TWSGRGEALQ ITDQKHLELV ALMTHFAVED KDDVRKGLAA FNEQTDWLIK HARLDRSKLT
     LHAANSFATL EVPEARLDMV RTGGALFGDT VPGRTEYKRA MQFKSRVAAV HSYPAGNTVG
     YDRTFTLARD SRLANITVGY SDGYRRVFTN KGHVLINGHR VPVVGKVSMN TLMVDVTDFP
     DVKGGNEVVL FGKQAGGEIT QAEMEEINGA LLADLYTVWG SSNPKILVD
//
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