GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0T7CM96_BORP1
LinkDB: A0A0T7CM96_BORP1
Original site: A0A0T7CM96_BORP1 
ID   A0A0T7CM96_BORP1        Unreviewed;       375 AA.
AC   A0A0T7CM96;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   23-MAY-2018, entry version 18.
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:CCJ62612.1};
GN   OrderedLocusNames=BN118_1187 {ECO:0000313|EMBL:CCJ62612.1};
OS   Bordetella pertussis (strain ATCC 9797 / DSM 5571 / NCTC 10739 /
OS   18323).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=568706 {ECO:0000313|EMBL:CCJ62612.1, ECO:0000313|Proteomes:UP000005250};
RN   [1] {ECO:0000313|EMBL:CCJ62612.1, ECO:0000313|Proteomes:UP000005250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9797 / DSM 5571 / NCTC 10739 / 18323
RC   {ECO:0000313|Proteomes:UP000005250};
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.,
RA   Liu M., Miller J.F., Sebaihia M., Bentley S.D., Parkhill J.,
RA   Harvill E.T.;
RT   "Comparative genomics of the classical Bordetella subspecies: the
RT   evolution and exchange of virulence-associated diversity amongst
RT   closely related pathogens.";
RL   BMC Genomics 13:545-545(2012).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|SAAS:SAAS00630646}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; HE965805; CCJ62612.1; -; Genomic_DNA.
DR   RefSeq; WP_014905624.1; NC_018518.1.
DR   ProteinModelPortal; A0A0T7CM96; -.
DR   EnsemblBacteria; CCJ62612; CCJ62612; BN118_1187.
DR   KEGG; bper:BN118_1187; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   BioCyc; BPER568706:G1HBS-1230-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000005250; 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   Gene3D; 2.40.37.10; -; 2.
DR   Gene3D; 3.20.20.10; -; 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   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; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005250};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:CCJ62612.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   ACT_SITE     44     44       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    270    270       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     139    139       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     318    318       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      44     44       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   375 AA;  39562 MW;  E8E1C911407F0012 CRC64;
     MPRPIFASIS QSALRHNLAT VRRHLDDVAA KADGTPPSIW AVIKANAYGH GIEQAVAGFS
     AAQGLAMLDL QEAVRCREAG WGGPILLLEG FFQPSDLEIV DRYHLATTVH TREQFDMLAH
     ARLSRRVDIM VKLNSGMNRL GFAPDAYGSA YARAQQLHEY GVVGGIGKMT HFACADGPQG
     VTQQMNVFNG ATAHLAGATS VCNSAATLRY ADLAVGHDGQ THWVRPGICL YGASPFADAQ
     AGAFGLIPAM TLRSELIAIQ DIPAGAAVGY GAIFRADRPM RIGVVACGYA DGYPRHAGTG
     MPLTVGGVRT RLVGRVSMDM LMVDLDPVPA AGIGTPVVLW GEDGPSVDEV AEAAGTIGYE
     LLCALAPRVP VRHEG
//
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