GenomeNet

Database: UniProt/TrEMBL
Entry: F2K6V4_PSEBN
LinkDB: F2K6V4_PSEBN
Original site: F2K6V4_PSEBN 
ID   F2K6V4_PSEBN            Unreviewed;       357 AA.
AC   F2K6V4;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 73.
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=PSEBR_a5506 {ECO:0000313|EMBL:AEA72031.1};
OS   Pseudomonas brassicacearum (strain NFM421).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=994484 {ECO:0000313|EMBL:AEA72031.1, ECO:0000313|Proteomes:UP000006692};
RN   [1] {ECO:0000313|EMBL:AEA72031.1, ECO:0000313|Proteomes:UP000006692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NFM421 {ECO:0000313|EMBL:AEA72031.1,
RC   ECO:0000313|Proteomes:UP000006692};
RX   PubMed=21515771; DOI=10.1128/JB.00411-11;
RA   Ortet P., Barakat M., Lalaouna D., Fochesato S., Barbe V., Vacherie B.,
RA   Santaella C., Heulin T., Achouak W.;
RT   "Complete genome sequence of a beneficial plant root-associated bacterium,
RT   Pseudomonas brassicacearum.";
RL   J. Bacteriol. 193:3146-3146(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NFM421;
RA   Ortet P., Barakat M., Lalaouna D., Fochesato S., Barbe V., Santaella C.,
RA   Heulin T., Achouak W.;
RT   "Complete Genome Sequence of a beneficial plant roots-associated bacterium
RT   Pseudomonas brassicacearum.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC       also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
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; CP002585; AEA72031.1; -; Genomic_DNA.
DR   RefSeq; WP_003206843.1; NC_015379.1.
DR   AlphaFoldDB; F2K6V4; -.
DR   STRING; 994484.PSEBR_a5506; -.
DR   GeneID; 57262454; -.
DR   KEGG; pba:PSEBR_a5506; -.
DR   HOGENOM; CLU_028393_1_0_6; -.
DR   OMA; WEILCGF; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000006692; 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   CDD; cd06827; PLPDE_III_AR_proteobact; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 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   NCBIfam; TIGR00492; alr; 1.
DR   PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR   PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
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; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}.
FT   DOMAIN          232..355
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        33
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        253
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         33
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   357 AA;  38849 MW;  AB3CA2F3F1E60B39 CRC64;
     MRPARALIDL QALRHNYQLA REITGAKALA VIKADAYGHG AVRCAEALQD TADGFAVACI
     EEALELRAGG IRGPILLLEG FFEASELPLI VEHDFWCVVH SLWQLEAIEK AALSQPITVW
     LKLDSGMHRV GLHPADYQAA YRRLLASGKV AKIVLMSHFA RADELHDPSS TEQLAIFDKA
     RQGLVAQISL RNSPAVLGWP QIPSDWVRPG IMLYGATPFD EPNAVASRLQ PVMTLESKII
     CVRELPAGEP VGYGARFVTT QPTRVGVVAM GYADGYPRQA PTGTPVLVDG QRSQLVGRVS
     MDMLCVDLTN VPQAGLGSTV ELWGKNILAS DVAKAADTIP YQIFCNLRRV PRLYSGH
//
DBGET integrated database retrieval system