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Database: UniProt/TrEMBL
Entry: I7C9X9_PSEPT
LinkDB: I7C9X9_PSEPT
Original site: I7C9X9_PSEPT 
ID   I7C9X9_PSEPT            Unreviewed;       357 AA.
AC   I7C9X9;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=dadX {ECO:0000313|EMBL:AFO48619.1};
GN   OrderedLocusNames=T1E_2780 {ECO:0000313|EMBL:AFO48619.1};
OS   Pseudomonas putida (strain DOT-T1E).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1196325 {ECO:0000313|EMBL:AFO48619.1, ECO:0000313|Proteomes:UP000006503};
RN   [1] {ECO:0000313|Proteomes:UP000006503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DOT-T1E {ECO:0000313|Proteomes:UP000006503};
RX   PubMed=23815283; DOI=10.1111/1751-7915.12061;
RA   Udaondo Z., Molina L., Daniels C., Gomez M.J., Molina-Henares M.A.,
RA   Matilla M.A., Roca A., Fernandez M., Duque E., Segura A., Ramos J.L.;
RT   "Metabolic potential of the organic-solvent tolerant Pseudomonas putida
RT   DOT-T1E deduced from its annotated genome.";
RL   Microb. Biotechnol. 6:598-611(2013).
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; CP003734; AFO48619.1; -; Genomic_DNA.
DR   AlphaFoldDB; I7C9X9; -.
DR   KEGG; ppx:T1E_2780; -.
DR   PATRIC; fig|1196325.3.peg.2767; -.
DR   HOGENOM; CLU_028393_1_0_6; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000006503; 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;  38682 MW;  9DD7EE38778C885C CRC64;
     MRPARALIDL QALRHNYRLA RELTGAKALA VIKADAYGHG AVRCALALEA EADGFAVACI
     EEALELRAAG INAPVLLLEG FFEASELALI AEHDLWCVVH SLWQLEAIEK TPLHKPLTVW
     LKLDSGMHRV GLHPKDYHDA YQRLLASGKV SRIVLMSHFA RADELDADAT AQQIAVFEAA
     RQGLAAECSL RNSPGVLGWP QAPSDWVRPG LMLYGATPFE VTQAEAARLQ PVMTLQSRVI
     SVRELPAGEP VGYGAKFVSP RPTRVGVVAM GYADGYPRQA PNGTPVLVAG KRTQLIGRVS
     MDMLSIDLTD VPQATVGSPV ELWGKQVLAS EVAAQAGTIP YQIFCNLKRV PRDYVGE
//
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