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Database: UniProt/TrEMBL
Entry: T1X3C1_VARPD
LinkDB: T1X3C1_VARPD
Original site: T1X3C1_VARPD 
ID   T1X3C1_VARPD            Unreviewed;       366 AA.
AC   T1X3C1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-SEP-2017, entry version 30.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=alr {ECO:0000313|EMBL:AGU47417.1};
GN   ORFNames=VAPA_1c02870 {ECO:0000313|EMBL:AGU47417.1};
OS   Variovorax paradoxus B4.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1246301 {ECO:0000313|EMBL:AGU47417.1, ECO:0000313|Proteomes:UP000016223};
RN   [1] {ECO:0000313|EMBL:AGU47417.1, ECO:0000313|Proteomes:UP000016223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:AGU47417.1,
RC   ECO:0000313|Proteomes:UP000016223};
RA   Schuldes J., Brandt U., Hiessl S., Wuebbeler J.H., Thuermer A.,
RA   Steinbuechel A., Daniel R.;
RT   "Genome sequence of Variovorax paradoxus B4.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|SAAS:SAAS00630646}.
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, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; CP003911; AGU47417.1; -; Genomic_DNA.
DR   RefSeq; WP_021004984.1; NC_022247.1.
DR   EnsemblBacteria; AGU47417; AGU47417; VAPA_1c02870.
DR   KEGG; vpd:VAPA_1c02870; -.
DR   PATRIC; fig|1246301.3.peg.292; -.
DR   KO; K01775; -.
DR   OrthoDB; POG091H022F; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000016223; Chromosome 1.
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 {ECO:0000313|Proteomes:UP000016223};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:AGU47417.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      233    363       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    254    254       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     130    130       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     302    302       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   366 AA;  39795 MW;  40A100C250C1032D CRC64;
     MPRPILATVH TAALRHNLDR ARRAAVDARV WAVVKANAYG HGIERVYEGL RGADGFALLD
     LAEAERVRAL GWRGPVLLLE GVFEARDLEL CSRLDLWHAV HCDEQIDMLA AHKTLKPQRV
     FLKMNSGMNR LGFTPERFGS AWTRLNALPQ VDEISLMTHF SDADGARGIA HQLEVFDRVT
     HDLPGERSIA NSAATLRHAR QTRGDWVRPG IVLYGSAPDF PEHDAAHWQL QPTMTLSTKL
     IGVQTLKAGD TIGYGSNFTA DGPLTIGVAA VGYADGYPRH CNTGTPVLVN GVRTRMVGRV
     SMDMITVDLT PVPDAKFGTE VTLWGRSAVT GAVLPIDEVA QAAGTVGYEL MCAVAPRVPF
     APADDE
//
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