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Database: UniProt/TrEMBL
Entry: Q6NJ45_CORDI
LinkDB: Q6NJ45_CORDI
Original site: Q6NJ45_CORDI 
ID   Q6NJ45_CORDI            Unreviewed;       382 AA.
AC   Q6NJ45;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-SEP-2017, entry version 112.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=DIP0568 {ECO:0000313|EMBL:CAE49080.1};
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=257309 {ECO:0000313|Proteomes:UP000002198};
RN   [1] {ECO:0000313|EMBL:CAE49080.1, ECO:0000313|Proteomes:UP000002198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis
RC   {ECO:0000313|Proteomes:UP000002198};
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA   Pallen M., Bentley S.D., Besra G.S., Churcher C., James K.D.,
RA   De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Moule S., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K., Thomson N.R., Unwin L., Whitehead S.,
RA   Barrell B.G.Parkhill.J.;
RT   "The complete genome sequence and analysis of Corynebacterium
RT   diphtheriae NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(2003).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201}.
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DR   EMBL; BX248355; CAE49080.1; -; Genomic_DNA.
DR   RefSeq; WP_010934388.1; NC_002935.2.
DR   ProteinModelPortal; Q6NJ45; -.
DR   EnsemblBacteria; CAE49080; CAE49080; DIP0568.
DR   KEGG; cdi:DIP0568; -.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002198; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002198};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002198}.
FT   DOMAIN      240    369       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    261    261       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     134    134       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     309    309       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   382 AA;  41235 MW;  E76C0DCBC3416E10 CRC64;
     MNLLETRISC DAIAANTRRL KDMVAPAQLM CVVKADGYNH GAPEVATVMA RNGADQFGVA
     TLAEAHQLRD AGITLPILCW IWSPEQDFSA AIDRDIDLAA VSMDHVRALI AEAMRRPAGT
     RVRVTVKIDT ELHRSGIDEA NWTEAFELLH ACPQVNVTGV FSHLACADDL ESDYTDHQAE
     VFRRAISAGR NVGLDLPVNH LAASPATLTR PDLHFDMVRP GLALYGHEPI AGLDHGLREA
     MTWIGSVTVV KPIAAGQGTS YNMTWHAPAD GYLCVVPVGY ADGLPRNVQG HLEVTIAGTR
     YPQVGRVCMD QIVVFLGDNS RGVAPGDEAI IFGPRDTQAM TVTELACATG TINYEILCRP
     TGRSHRTYSA LDAVAPTHPT ES
//
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