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}.
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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
//