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Database: UniProt/TrEMBL
Entry: A0A0U3DSF7_9BURK
LinkDB: A0A0U3DSF7_9BURK
Original site: A0A0U3DSF7_9BURK 
ID   A0A0U3DSF7_9BURK        Unreviewed;       370 AA.
AC   A0A0U3DSF7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   28-FEB-2018, entry version 14.
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=AT984_20055 {ECO:0000313|EMBL:ALT79140.1};
OS   Paucibacter sp. KCTC 42545.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Paucibacter.
OX   NCBI_TaxID=1768242 {ECO:0000313|EMBL:ALT79140.1, ECO:0000313|Proteomes:UP000056576};
RN   [1] {ECO:0000313|EMBL:ALT79140.1, ECO:0000313|Proteomes:UP000056576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 42545 {ECO:0000313|EMBL:ALT79140.1,
RC   ECO:0000313|Proteomes:UP000056576};
RA   Kim S.-G., Lee Y.-J.;
RT   "Complete genome of Paucibacter sp. KCTC 42545.";
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}.
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DR   EMBL; CP013692; ALT79140.1; -; Genomic_DNA.
DR   RefSeq; WP_058721614.1; NZ_CP013692.1.
DR   EnsemblBacteria; ALT79140; ALT79140; AT984_20055.
DR   KEGG; pkt:AT984_20055; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000056576; 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:UP000056576};
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:UP000056576}.
FT   DOMAIN      233    362       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   370 AA;  40244 MW;  1966FB4AC8C09D6D CRC64;
     MPRPIEAHIH LPAIAHNLAR ARARAPDAKL WAVVKANAYG HGIAHAYEAM RSADGFALLD
     FAEAKLLREL GWRGPILLLE GCFEARDLEL CSRLKLWHTV HCEQQIDWLA MHKTHEPHRV
     FLKLNSGMNR LGFTPQAFRA AWTRLNVLPQ VDEISLMTHF SDADGEIGIE AQVAAFERVC
     ADLPGERSLS NSAAILRHSE RLRSDWVRAG ILTYGGVPDY PVHDQGFWDL QPAMSLRSKI
     IAVQHLQPGD TVGYGSSFTA TAPMRIGVVA CGYADGYPRH CPTGTPVLVD GQRCSTVGRV
     SMDMLAVDLT ALPKAGAGSE VTLWGRSSKG QVLPIDEVAQ AAKTIGYELM CALALRVPVT
     VDHGAAGLAG
//
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