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Database: UniProt
Entry: O86786
LinkDB: O86786
Original site: O86786 
ID   ALR_STRCO               Reviewed;         391 AA.
AC   O86786;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JAN-2019, entry version 123.
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; OrderedLocusNames=SCO4745; ORFNames=SC6G4.23;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
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; AL939121; CAA20401.1; -; Genomic_DNA.
DR   PIR; T35574; T35574.
DR   RefSeq; NP_628903.1; NC_003888.3.
DR   RefSeq; WP_011029835.1; NC_003888.3.
DR   PDB; 5FAC; X-ray; 2.80 A; A/B/C/D=1-391.
DR   PDB; 5FAG; X-ray; 1.51 A; A/B/C/D=1-391.
DR   PDB; 5FAJ; X-ray; 1.64 A; A/B/C/D=1-391.
DR   PDBsum; 5FAC; -.
DR   PDBsum; 5FAG; -.
DR   PDBsum; 5FAJ; -.
DR   ProteinModelPortal; O86786; -.
DR   SMR; O86786; -.
DR   STRING; 100226.SCO4745; -.
DR   EnsemblBacteria; CAA20401; CAA20401; CAA20401.
DR   GeneID; 1100186; -.
DR   KEGG; sco:SCO4745; -.
DR   PATRIC; fig|100226.15.peg.4817; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   InParanoid; O86786; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   PhylomeDB; O86786; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001973; 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    391       Alanine racemase.
FT                                /FTId=PRO_0000114580.
FT   ACT_SITE     46     46       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    283    283       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     148    148       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     331    331       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      46     46       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   HELIX         3     12       {ECO:0000244|PDB:5FAG}.
FT   TURN         13     15       {ECO:0000244|PDB:5FAG}.
FT   STRAND       16     21       {ECO:0000244|PDB:5FAG}.
FT   HELIX        22     35       {ECO:0000244|PDB:5FAG}.
FT   STRAND       39     44       {ECO:0000244|PDB:5FAG}.
FT   HELIX        46     50       {ECO:0000244|PDB:5FAG}.
FT   HELIX        54     63       {ECO:0000244|PDB:5FAG}.
FT   STRAND       68     73       {ECO:0000244|PDB:5FAG}.
FT   HELIX        74     81       {ECO:0000244|PDB:5FAG}.
FT   STRAND       92     95       {ECO:0000244|PDB:5FAG}.
FT   HELIX       104    109       {ECO:0000244|PDB:5FAG}.
FT   STRAND      113    116       {ECO:0000244|PDB:5FAG}.
FT   HELIX       119    132       {ECO:0000244|PDB:5FAG}.
FT   STRAND      136    142       {ECO:0000244|PDB:5FAG}.
FT   STRAND      144    146       {ECO:0000244|PDB:5FAJ}.
FT   STRAND      148    151       {ECO:0000244|PDB:5FAG}.
FT   HELIX       155    169       {ECO:0000244|PDB:5FAG}.
FT   STRAND      172    179       {ECO:0000244|PDB:5FAG}.
FT   HELIX       191    209       {ECO:0000244|PDB:5FAG}.
FT   STRAND      215    218       {ECO:0000244|PDB:5FAG}.
FT   HELIX       222    227       {ECO:0000244|PDB:5FAG}.
FT   HELIX       229    231       {ECO:0000244|PDB:5FAG}.
FT   HELIX       239    242       {ECO:0000244|PDB:5FAG}.
FT   TURN        249    251       {ECO:0000244|PDB:5FAG}.
FT   HELIX       255    257       {ECO:0000244|PDB:5FAG}.
FT   STRAND      263    268       {ECO:0000244|PDB:5FAG}.
FT   STRAND      270    275       {ECO:0000244|PDB:5FAG}.
FT   STRAND      280    282       {ECO:0000244|PDB:5FAJ}.
FT   HELIX       283    285       {ECO:0000244|PDB:5FAG}.
FT   STRAND      290    299       {ECO:0000244|PDB:5FAG}.
FT   HELIX       302    304       {ECO:0000244|PDB:5FAG}.
FT   HELIX       308    310       {ECO:0000244|PDB:5FAG}.
FT   TURN        311    313       {ECO:0000244|PDB:5FAG}.
FT   STRAND      315    318       {ECO:0000244|PDB:5FAG}.
FT   STRAND      321    325       {ECO:0000244|PDB:5FAG}.
FT   STRAND      334    337       {ECO:0000244|PDB:5FAG}.
FT   STRAND      348    355       {ECO:0000244|PDB:5FAG}.
FT   HELIX       362    368       {ECO:0000244|PDB:5FAG}.
FT   HELIX       373    378       {ECO:0000244|PDB:5FAG}.
FT   STRAND      386    389       {ECO:0000244|PDB:5FAG}.
SQ   SEQUENCE   391 AA;  41200 MW;  24754AC1385DCA1B CRC64;
     MSETTARRDA DAVLRARAEI DLAALRANVR ALRERAPGAA LMAVVKADAY GHGAIPCARA
     AVAAGATWLG TATPQEALAL RAAEPGLPDD VRIMCWLWTP GGPWREAVEA RLDVSVSAMW
     AMEEVTGAAR AAGVPARVQL KADTGLGRGG CQPGADWERL VGAALRAEEE GLLRVTGLWS
     HFACADEPGH PSIAAQLTRF REMTAYAEQR GLRPEVRHIA NSPATLTLPD AHFDLVRPGI
     AMYGVSPSPE IGTPADFGLR PVMTLAASLA LVKQVPGGHG VSYGHHYTTP GETTLGLVPL
     GYADGIPRHA SSSGPVLVDG KWRTVAGRIA MDQFVVDLGG DRPEPGAEAV LFGPGDRGEP
     TAEDWAQAAG TIAYEIVTRI GSRVPRVYVN E
//
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