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Database: UniProt/TrEMBL
Entry: C5AJN3_BURGB
LinkDB: C5AJN3_BURGB
Original site: C5AJN3_BURGB 
ID   C5AJN3_BURGB            Unreviewed;       375 AA.
AC   C5AJN3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 99.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=bglu_2g17750 {ECO:0000313|EMBL:ACR32113.1};
OS   Burkholderia glumae (strain BGR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR32113.1, ECO:0000313|Proteomes:UP000002187};
RN   [1] {ECO:0000313|EMBL:ACR32113.1, ECO:0000313|Proteomes:UP000002187}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGR1 {ECO:0000313|EMBL:ACR32113.1,
RC   ECO:0000313|Proteomes:UP000002187};
RX   PubMed=19329631; DOI=10.1128/JB.00349-09;
RA   Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT   "Complete genome sequence of Burkholderia glumae BGR1.";
RL   J. Bacteriol. 191:3758-3759(2009).
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; CP001504; ACR32113.1; -; Genomic_DNA.
DR   RefSeq; WP_015877796.1; NC_012721.2.
DR   AlphaFoldDB; C5AJN3; -.
DR   STRING; 626418.bglu_2g17750; -.
DR   KEGG; bgl:bglu_2g17750; -.
DR   PATRIC; fig|626418.3.peg.2089; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_1_0_4; -.
DR   OMA; LMAVQHI; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002187; Chromosome 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000002187}.
FT   DOMAIN          231..355
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        35
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        252
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         35
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   375 AA;  40568 MW;  47DB39FFA521D5A3 CRC64;
     MPRPIVAQIR PAAVRHNLAI IRRKAAGTRI WAVVKANAYG HGIERIYPAL ADADGIALLD
     LDEAVRVREL GWTRPVLLLE GLFDASDVAV ADRYRLTVAV HGEEQLDMLA SARPSRPIDI
     QLKMNSGMNR LGFRPSAFRA AWERASATPA VGRIALMTHF ANADEGEVAW QTQQFDAATE
     GLPGERSLSN SAAVLWHPDA HRDWVRPGTI LYGASPTGAT RHIADTGLVP AMTLTSRLIG
     VQTIEENETV GYGRRFAAKR TMRIGVVACG YADGYPRHAQ TGTPIAVDGI VTRVVGRVSM
     DMLTVDLTPC PNARVGSSVE LWGEQVRVDD VAEASGTIGY ELMCAIARRV PVVVEPLVDA
     PALDMPVLRT GSYGR
//
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