GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0U3MSA4_9BURK
LinkDB: A0A0U3MSA4_9BURK
Original site: A0A0U3MSA4_9BURK 
ID   A0A0U3MSA4_9BURK        Unreviewed;       367 AA.
AC   A0A0U3MSA4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   28-FEB-2018, entry version 13.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   ORFNames=RD2015_253 {ECO:0000313|EMBL:ALV04756.1};
OS   Roseateles depolymerans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Roseateles.
OX   NCBI_TaxID=76731 {ECO:0000313|EMBL:ALV04756.1, ECO:0000313|Proteomes:UP000060699};
RN   [1] {ECO:0000313|EMBL:ALV04756.1, ECO:0000313|Proteomes:UP000060699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 42856 {ECO:0000313|EMBL:ALV04756.1,
RC   ECO:0000313|Proteomes:UP000060699};
RA   Kim K.M.;
RT   "Complete genome of Roseateles depolymerans KCTC 42856.";
RL   Submitted (DEC-2015) 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP013729; ALV04756.1; -; Genomic_DNA.
DR   RefSeq; WP_058933342.1; NZ_CP013729.1.
DR   EnsemblBacteria; ALV04756; ALV04756; RD2015_253.
DR   KEGG; rdp:RD2015_253; -.
DR   PATRIC; fig|76731.3.peg.254; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000060699; 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; -; 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:UP000060699};
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:UP000060699}.
FT   DOMAIN      235    364       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    256    256       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     304    304       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   367 AA;  40168 MW;  B51565B1D3484A75 CRC64;
     MPRPIEALIH QPALAHNLHR ARECAPDAQV FAIVKANAYG HGIDRVFDAF RAADGFALLD
     LDEAQRIRDL GWRGPILLLE GCFEPRDLEL CSRLRLWHAV HSEQQIDWLA MHKTHEPHRV
     FLKLNSGMNR LGFTPSGFRA AWTRLNALPQ VDEISLMTHF SDADGPKGID RQLAVFQEAT
     ADLPGERSLS NSAAVLRHSE RAGVRADWVR AGIMSYGSAP DFPEHDIRHW NLQPTMTLRS
     KVLAVQALQP GDTVGYGSTF VADRPMRIGT VACGYADGYP RHAGTGTPVL VGGQRTRTVG
     RVSMDMLAVD LTDLPQLGAG SEVTLWGQGP NGSMLSIDEV AAAAGTIGYE LMCALARRVP
     VHLDPLT
//
DBGET integrated database retrieval system