GenomeNet

Database: UniProt
Entry: Q9PP26
LinkDB: Q9PP26
Original site: Q9PP26 
ID   ALR_CAMJE               Reviewed;         328 AA.
AC   Q9PP26; Q0P9Z3;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   05-DEC-2018, entry version 107.
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=Cj0905c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 /
OS   NCTC 11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W.,
RA   Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M.,
RA   Whitehead S., Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL35026.1; -; Genomic_DNA.
DR   PIR; A81364; A81364.
DR   RefSeq; WP_002852617.1; NC_002163.1.
DR   RefSeq; YP_002344304.1; NC_002163.1.
DR   ProteinModelPortal; Q9PP26; -.
DR   SMR; Q9PP26; -.
DR   IntAct; Q9PP26; 11.
DR   STRING; 192222.Cj0905c; -.
DR   PaxDb; Q9PP26; -.
DR   PRIDE; Q9PP26; -.
DR   EnsemblBacteria; CAL35026; CAL35026; Cj0905c.
DR   GeneID; 905209; -.
DR   KEGG; cje:Cj0905c; -.
DR   PATRIC; fig|192222.6.peg.889; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   KO; K01775; -.
DR   OMA; NTVMVDV; -.
DR   BioCyc; CJEJ192222:G1G1F-862-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000799; 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   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    328       Alanine racemase.
FT                                /FTId=PRO_0000114505.
FT   ACT_SITE     33     33       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    237    237       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     118    118       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     283    283       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      33     33       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   328 AA;  37256 MW;  1F82682833905D22 CRC64;
     MSLIKIDQKA YEYNLRHIAK KIGSFQRLIC VFKDNAYGHG AKLLAPLAKN LGVSFVAVKS
     EEEAREIEEF FENILILSHR PHGNENSRFI YALNDISQVK NYKQDIKIHL KIDTGMHRNG
     ICVENLEHAI NLIQGSDLKL TGMFTHFASA DEMDGSFFVQ KENFQKAKKI VKKYFSNLLF
     HSYNSAALFR GKIPEDEYCR VGLVQFGYGD SNLKRVLSLY AHRLSQRILQ KGQSIGYGGI
     FTAAKDMEVA TYDLGYADGL FRYNGRGELV LGNGKAMLGK MSMDSFSCEN SGEEICVFKD
     ADIWADFFHT INYEILVKLN PNIQRVLV
//
DBGET integrated database retrieval system