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Database: UniProt
Entry: Q8FS13
LinkDB: Q8FS13
Original site: Q8FS13 
ID   ALR_COREF               Reviewed;         367 AA.
AC   Q8FS13;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   13-FEB-2019, entry version 99.
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=CE0593;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM
OS   11189 / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E.,
RA   Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K.,
RA   Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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; BA000035; BAC17403.1; -; Genomic_DNA.
DR   RefSeq; WP_006769730.1; NZ_GG700687.1.
DR   ProteinModelPortal; Q8FS13; -.
DR   SMR; Q8FS13; -.
DR   STRING; 196164.HMPREF0290_1138; -.
DR   EnsemblBacteria; BAC17403; BAC17403; BAC17403.
DR   KEGG; cef:CE0593; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; GCF_000160795-HMP:HMPREF0290_RS10405-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001409; 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; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    367       Alanine racemase.
FT                                /FTId=PRO_1000065983.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    258    258       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     131    131       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     306    306       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   367 AA;  39352 MW;  B07005E2CF893D6A CRC64;
     MNLLTTRIDL DAIAHNTRLL KNRVGAAKLM AVVKADGYNH GMDRVAPVMA ANGADAFGVA
     TIAEALALRA TGITTPILCW IWSPEQDWAA AVEAGIDLAV ISPRHARVLV DAPPTSRAIR
     VSVKVDTALH RSGVDEQDWD AVFTLLRDCG HIEVTGLFTH LSCADEPGNP ETDHQAETFR
     RAIDRARALG LEVPENHLCN SPATLTRPDL HMDMVRPGVA LYGLEPIPGL DHGLRPAMTW
     AGAITVVKPI RKGEGTSYGL TWRAEADGFV AVVPAGYADG VPRAAQDHLR VHVNGHDYPQ
     VGRVCMDQFV IFLGDNPHGV TAGDEAVIFG GTGMSATELA DALATINYEV ICRPTGRTVR
     DYTGEGK
//
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