ID   K0MFB9_BORPB            Unreviewed;       387 AA.
AC   K0MFB9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=Alanine racemase, catabolic {ECO:0000313|EMBL:CCJ48739.1};
DE            EC=5.1.1.1 {ECO:0000313|EMBL:CCJ48739.1};
GN   Name=alr {ECO:0000313|EMBL:CCJ48739.1};
GN   Synonyms=dadB {ECO:0000313|EMBL:CCJ48739.1};
GN   OrderedLocusNames=BN117_1406 {ECO:0000313|EMBL:CCJ48739.1};
OS   Bordetella parapertussis (strain Bpp5).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1208660 {ECO:0000313|EMBL:CCJ48739.1, ECO:0000313|Proteomes:UP000008035};
RN   [1] {ECO:0000313|EMBL:CCJ48739.1, ECO:0000313|Proteomes:UP000008035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bpp5 {ECO:0000313|EMBL:CCJ48739.1,
RC   ECO:0000313|Proteomes:UP000008035};
RX   PubMed=23051057; DOI=10.1186/1471-2164-13-545;
RA   Park J., Zhang Y., Buboltz A.M., Zhang X., Schuster S.C., Ahuja U., Liu M.,
RA   Miller J.F., Sebaihia M., Bentley S.D., Parkhill J., Harvill E.T.;
RT   "Comparative genomics of the classical Bordetella subspecies: the evolution
RT   and exchange of virulence-associated diversity amongst closely related
RT   pathogens.";
RL   BMC Genomics 13:545-545(2012).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR600821-50};
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DR   EMBL; HE965803; CCJ48739.1; -; Genomic_DNA.
DR   RefSeq; WP_015039330.1; NC_018828.1.
DR   RefSeq; YP_006895388.1; NC_018828.1.
DR   AlphaFoldDB; K0MFB9; -.
DR   GeneID; 56479674; -.
DR   KEGG; bpar:BN117_1406; -.
DR   HOGENOM; CLU_028393_1_0_4; -.
DR   Proteomes; UP000008035; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.10; Alanine 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   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:CCJ48739.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR600821-50}.
FT   DOMAIN          251..376
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         49
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   387 AA;  41465 MW;  706F846FF0EF2A75 CRC64;
     MPLASDPFDA PIPGLHACID PIAVAHNLEV LRQRLGVGVD GPRIWATVKA DAYGHGLHNV
     LPGLRAADGI AVRHLHEAHQ CRRVGWRGPI MVYAGLTHER EAALLTLQQL HLVITDMTQL
     EWLPGKPLYA CAPWVWLRYI GATRLGGLDA GEYRRAYARC RELQQHGALR GVGHLNHYAN
     AASVGDLERE HADFEACIRG LPGPVSTCNS AASCVMPTMA ARTDWVRPGL ALYGVSPIPD
     RVGRDLGLRP AMTLRSTLCA TQKLPAGASV GYGCAFVADQ PMALGLVRCG YGDGYPHNPR
     ASFPVQVDGV LTRTVGRISM DLMAVDLRPI PAAARGAPVV LWGSPQLPVE HIAHAADTIA
     AELLTGLTAR VPLMRADHAA LLRGPLA
//