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Database: UniProt/TrEMBL
Entry: A0A1W0ZTJ8_9BURK
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Original site: A0A1W0ZTJ8_9BURK 
ID   A0A1W0ZTJ8_9BURK        Unreviewed;       356 AA.
AC   A0A1W0ZTJ8;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   28-FEB-2018, entry version 5.
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:SAK17419.1};
GN   ORFNames=CA830_14660 {ECO:0000313|EMBL:OXH90754.1}, CA831_16300
GN   {ECO:0000313|EMBL:OXH88758.1}, UA18_01783
GN   {ECO:0000313|EMBL:SAK17419.1};
OS   Burkholderia multivorans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=87883 {ECO:0000313|EMBL:SAK17419.1, ECO:0000313|Proteomes:UP000196218};
RN   [1] {ECO:0000313|EMBL:SAK17419.1, ECO:0000313|Proteomes:UP000196218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29311 {ECO:0000313|EMBL:SAK17419.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K.,
RA   Barbian K., Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OXH88758.1, ECO:0000313|Proteomes:UP000214593, ECO:0000313|Proteomes:UP000214680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSOPR54 {ECO:0000313|EMBL:OXH90754.1,
RC   ECO:0000313|Proteomes:UP000214680}, and DSOPR57
RC   {ECO:0000313|EMBL:OXH88758.1, ECO:0000313|Proteomes:UP000214593};
RA   Ong C.E.L., Ng J.L.Y.;
RT   "Draft genome sequences of two Burkholderia multivorans strains with
RT   novel strain type, isolated from soil samples in Singapore.";
RL   Submitted (MAY-2017) 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; NGKL01000609; OXH88758.1; -; Genomic_DNA.
DR   EMBL; NGKK01000609; OXH90754.1; -; Genomic_DNA.
DR   EMBL; FKJW01000003; SAK17419.1; -; Genomic_DNA.
DR   RefSeq; WP_035951144.1; NZ_LPJZ01000002.1.
DR   KEGG; bmk:DM80_2937; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000196218; Unassembled WGS sequence.
DR   Proteomes; UP000214593; Unassembled WGS sequence.
DR   Proteomes; UP000214680; Unassembled WGS sequence.
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; -; 2.
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:UP000196218,
KW   ECO:0000313|Proteomes:UP000214593, ECO:0000313|Proteomes:UP000214680};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:SAK17419.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      232    356       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    253    253       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     301    301       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   356 AA;  38089 MW;  AF0632799B213F8B CRC64;
     MPRPISATIH TAALANNLSV VRRYAGPSKV WAVVKANAYG HGLARVFPGL RGTDGFGLLD
     LDEAVKLREL GWAGPILLLE GFFRSTDIDV IDRYSLTTTV HNDEQMRMLE TARLSKPVNV
     QLKMNSGMNR LGYAPEKYRA AWERARACPS IGQITLMTHF SDADNERGVA EQLATFERGA
     ANIAGARCLA NSAAVLWHPD THFDWVRPGI VLYGASPSGL SSDIADTGLK PAMTLSSELI
     AVQSIGKGQA IGYGSTFAAP APMRIGVVAC GYADGYPRVA PEGTPVIVDG IRTRIVGRVS
     MDMITVDLTP CPQAGVGARV ELWGNALSID DVARHCGTIG YELMCAVAAR VPVRAE
//
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