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Database: UniProt/TrEMBL
Entry: A0A1V0BCT5_9BURK
LinkDB: A0A1V0BCT5_9BURK
Original site: A0A1V0BCT5_9BURK 
ID   A0A1V0BCT5_9BURK        Unreviewed;       372 AA.
AC   A0A1V0BCT5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-SEP-2017, entry version 4.
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=B5M06_05165 {ECO:0000313|EMBL:AQZ97746.1};
OS   Comamonas kerstersii.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=225992 {ECO:0000313|EMBL:AQZ97746.1};
RN   [1] {ECO:0000313|EMBL:AQZ97746.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=8943 {ECO:0000313|EMBL:AQZ97746.1};
RA   Zheng B.;
RT   "Rapid Whole Genome Sequencing of Comamonas kerstersii Causing
RT   Continuous ambulatory Peritoneal Dialysis-Associated Peritonitis.";
RL   Submitted (MAR-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}.
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}.
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DR   EMBL; CP020121; AQZ97746.1; -; Genomic_DNA.
DR   RefSeq; WP_054067964.1; NZ_LFYP01000148.1.
DR   KEGG; cke:B5M06_05165; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
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   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}.
FT   DOMAIN      235    365       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   372 AA;  40469 MW;  06949704ACF4A602 CRC64;
     MPRPILATIH PQALRHNLEQ VRKAAPDAKL MCMVKANAYG HGLEHAFAGL RAADGFAVLE
     IAEAQRLRAM DWRGPILLIE GVFEPRDLEM CSRLGLWHTV HCDRQIDWLA AHKTQVPHRV
     FLKMNSGMNR LGFTPERFRS AYARLNALTQ VEEISFITHF SDADGPRGTA HQRAVFERAT
     HDLPGERTLC NSAASLLEAS DEHLRGDWVR PGIVLFGSSP DYPAHTAQDW NLQPAMTLSA
     QVIGTQQLQA GDTVGYGSTF TATGPMHIGV VSCGYADGYP RLCGTDTPVL VNGVRTRLLG
     RVSMDMLCVD LTPVPGAGLG SEVVLWGKSP RTGAMLSIDE VAAAAGTVGY ELMCAVAARV
     PMVNDEEATP RK
//
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