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Database: UniProt
Entry: Q5ZSJ5_LEGPH
LinkDB: Q5ZSJ5_LEGPH
Original site: Q5ZSJ5_LEGPH 
ID   Q5ZSJ5_LEGPH            Unreviewed;       384 AA.
AC   Q5ZSJ5;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Metal-activated pyridoxal enzyme {ECO:0000313|EMBL:AAU28582.1};
GN   OrderedLocusNames=lpg2522 {ECO:0000313|EMBL:AAU28582.1};
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624 {ECO:0000313|EMBL:AAU28582.1, ECO:0000313|Proteomes:UP000000609};
RN   [1] {ECO:0000313|EMBL:AAU28582.1, ECO:0000313|Proteomes:UP000000609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513
RC   {ECO:0000313|Proteomes:UP000000609};
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(2004).
CC   -!- SIMILARITY: Belongs to the DSD1 family.
CC       {ECO:0000256|ARBA:ARBA00005323}.
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DR   EMBL; AE017354; AAU28582.1; -; Genomic_DNA.
DR   RefSeq; YP_096529.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZSJ5; -.
DR   STRING; 272624.lpg2522; -.
DR   PaxDb; 272624-lpg2522; -.
DR   KEGG; lpn:lpg2522; -.
DR   PATRIC; fig|272624.6.peg.2680; -.
DR   eggNOG; COG3616; Bacteria.
DR   HOGENOM; CLU_031639_2_1_6; -.
DR   OrthoDB; 9772497at2; -.
DR   Proteomes; UP000000609; 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; D-SERINE DEHYDRATASE; 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:UP000000609}.
FT   DOMAIN          275..367
FT                   /note="D-serine dehydratase-like"
FT                   /evidence="ECO:0000259|SMART:SM01119"
SQ   SEQUENCE   384 AA;  43077 MW;  61CB25B2D34225D7 CRC64;
     MNFVMNYLMK EKYIGLHKIE LNTPCLVIDY EKLKYNLKVM QQHGFEWGIG IRPHCKTHKC
     TQIARLQLEY GAIGISAAKL SEAEVLVSKQ ITNVLITSPI VSEAKYSRLF NCLKSAPDLM
     LVVDGKDNIR MLNELGKSLN QPVYVLLDID SGIGRTGINP EVALEYGHFI NSMNWLKLKG
     IQCYAGHLQH IQNYEERKAF SLRIMDMASR IVKSFRDANL PCEILTGTGT GTFDIDVEAS
     EVTEIQPGSY AVMDVEYGSI GSKNNPSSFQ PFKNSMTLLT SVISSNRKEH ATVDAGTKSI
     YVDPHHKPHI ISHPGLVYDW GGFGDEHGKV FSCEGGSHFL QNGDVLELIV PHCDPTINLY
     DKFYITENNV VVDIWDIDMR GKSQ
//
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