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Database: UniProt
Entry: Q9JYC4
LinkDB: Q9JYC4
Original site: Q9JYC4 
ID   ALR_NEIMB               Reviewed;         352 AA.
AC   Q9JYC4;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JAN-2019, entry version 114.
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=NMB1651;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C.,
RA   Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F.,
RA   Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D.,
RA   Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D.,
RA   Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E.,
RA   Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M.,
RA   Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M.,
RA   Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R.,
RA   Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(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; AE002098; AAF42000.1; -; Genomic_DNA.
DR   PIR; B81059; B81059.
DR   RefSeq; NP_274656.1; NC_003112.2.
DR   RefSeq; WP_002224993.1; NC_003112.2.
DR   ProteinModelPortal; Q9JYC4; -.
DR   SMR; Q9JYC4; -.
DR   STRING; 122586.NMB1651; -.
DR   PaxDb; Q9JYC4; -.
DR   PRIDE; Q9JYC4; -.
DR   EnsemblBacteria; AAF42000; AAF42000; NMB1651.
DR   GeneID; 903465; -.
DR   KEGG; nme:NMB1651; -.
DR   PATRIC; fig|122586.8.peg.2124; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   BioCyc; NMEN122586:G1G1B-1603-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000425; 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    352       Alanine racemase.
FT                                /FTId=PRO_0000114541.
FT   ACT_SITE     33     33       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    250    250       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     129    129       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     298    298       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   352 AA;  38820 MW;  0AC586A9E12860E6 CRC64;
     MRPLNVQIRL GNLRHNYRIL KEMHGGKLLA VVKADAYGHG AVRCAFALAD LADGFAVATI
     DEGIRLRESG ITHPIVLLEG VFEASEYEAV EQYSLWPAVG NQWQLEALLI RHWKKTVKVW
     LKMDSGMHRT GFFPHDYASA YAALKQSEYV DSIVKFSHFS CADEPESGMT EIQMEAFDLG
     TEGLEGEESL ANSAAILNVP EARRDWGRAG LALYGISPFG GGDDRLKPVM RLSTRIFGER
     VLQPHSPIGY GATFYTSKST RVGLIACGYA DGYPRRAPSN SPVAVDGKLT RVIGRVSMDM
     MTIELDASQE GLGHEVELWG DTVNINTVAE AAGTIPYELM CNIKRAKFTY IE
//
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