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Database: UniProt
Entry: Q2KTM5_BORA1
LinkDB: Q2KTM5_BORA1
Original site: Q2KTM5_BORA1 
ID   Q2KTM5_BORA1            Unreviewed;       337 AA.
AC   Q2KTM5;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=Low-specificity D-threonine aldolase {ECO:0000313|EMBL:CAJ50985.1};
GN   OrderedLocusNames=BAV3375 {ECO:0000313|EMBL:CAJ50985.1};
OS   Bordetella avium (strain 197N).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ50985.1, ECO:0000313|Proteomes:UP000001977};
RN   [1] {ECO:0000313|EMBL:CAJ50985.1, ECO:0000313|Proteomes:UP000001977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N {ECO:0000313|EMBL:CAJ50985.1,
RC   ECO:0000313|Proteomes:UP000001977};
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
CC   -!- SIMILARITY: Belongs to the DSD1 family.
CC       {ECO:0000256|ARBA:ARBA00005323}.
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DR   EMBL; AM167904; CAJ50985.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2KTM5; -.
DR   STRING; 360910.BAV3375; -.
DR   KEGG; bav:BAV3375; -.
DR   eggNOG; COG3616; Bacteria.
DR   HOGENOM; CLU_031639_2_0_4; -.
DR   OMA; KLVPGHC; -.
DR   Proteomes; UP000001977; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProt.
DR   CDD; cd06819; PLPDE_III_LS_D-TA; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   Gene3D; 2.40.37.20; D-serine dehydratase-like domain; 1.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR026956; D-ser_dehydrat-like_dom.
DR   InterPro; IPR042208; D-ser_dehydrat-like_sf.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR28004:SF2; ZGC:162816; 1.
DR   PANTHER; PTHR28004; ZGC:162816-RELATED; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   Pfam; PF14031; D-ser_dehydrat; 1.
DR   SMART; SM01119; D-ser_dehydrat; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001977}.
FT   DOMAIN          232..320
FT                   /note="D-serine dehydratase-like"
FT                   /evidence="ECO:0000259|SMART:SM01119"
SQ   SEQUENCE   337 AA;  35639 MW;  21F381930C356968 CRC64;
     MQQWADRHGL ALRPHAKAHK CPEIARRQLA LGARGICCQK VSEALPFLDA GIRDIHISNE
     VVGPAKLALL AQLALRADVS VCVDNMSNLH ALAAAVAQVG ARITVLVEVD VGQGRCGVTD
     DHDVLALARA AEAMQGLRFG GLQAYHGAMQ HVRSHAERAA MSAQAAIRAA GYASLLRAYG
     ITCERITGGG TGSAEFDAAS GVYTELQAGS YAFMDADYGA NEWSDTLSFG TSLFLLSTVM
     STPAPERVVL DAGLKSTTIE CGLPRIQGRP GLVYVAANDE HGVVRVQDGA QAPALGEVLK
     LVVPHVDPCF NLHDTLVTYR DDTVVGLWPI AARGLSR
//
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