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Database: UniProt
Entry: A8AVC4
LinkDB: A8AVC4
Original site: A8AVC4 
ID   ALR_STRGC               Reviewed;         368 AA.
AC   A8AVC4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   16-JAN-2019, entry version 78.
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=SGO_0418;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1
OS   / DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/JB.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in
RT   response to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
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; CP000725; ABV09604.1; -; Genomic_DNA.
DR   RefSeq; WP_011999929.1; NC_009785.1.
DR   ProteinModelPortal; A8AVC4; -.
DR   SMR; A8AVC4; -.
DR   STRING; 467705.SGO_0418; -.
DR   EnsemblBacteria; ABV09604; ABV09604; SGO_0418.
DR   GeneID; 25051177; -.
DR   KEGG; sgo:SGO_0418; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   BioCyc; SGOR467705:G1G95-429-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001131; 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    368       Alanine racemase.
FT                                /FTId=PRO_1000085508.
FT   ACT_SITE     40     40       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    263    263       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     136    136       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     310    310       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      40     40       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   368 AA;  39876 MW;  3E1ADC34EBC31776 CRC64;
     MKTSIHRPSQ ALVDLSAIHF NIEQLKAHLP QDVEKWAVVK ANAYGHGAVA VSSYIDDIVD
     GFCVSNIDEA LELREGGLDK KILILGVSAI EVVPLAIQNK ITLTVASLEW LDLLEASSLS
     LQGLVVHLKV DSGMGRIGFR DRQPLQEAIN RLQVAGVQVE GIFTHFATAD EADASKFEEQ
     LACFKGILAE LDALPPIIHA SNSATSLWHT DTVMNAVRLG DIIYGLNPSG SVLELPYDIK
     PALSLVSELV HVKEVEAGAD VGYGATYTAD EGQFIGTIPL GYADGWTRDM QGFDVLIDGQ
     RCPIVGRISM DQITVRLPEK YPLGTPVVFI GKSGTESISA TDVAEKRGTI NYEVVCLISD
     RVPRIYKN
//
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