SDHD_ECOL6
ID SDHD_ECOL6 Reviewed; 442 AA.
AC Q8FFF4;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=D-serine dehydratase {ECO:0000255|HAMAP-Rule:MF_01030};
DE EC=4.3.1.18 {ECO:0000255|HAMAP-Rule:MF_01030};
DE AltName: Full=D-serine deaminase {ECO:0000255|HAMAP-Rule:MF_01030};
DE Short=DSD {ECO:0000255|HAMAP-Rule:MF_01030};
GN Name=dsdA {ECO:0000255|HAMAP-Rule:MF_01030}; OrderedLocusNames=c2901;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12823810; DOI=10.1046/j.1365-2958.2003.03543.x;
RA Roesch P.L., Redford P., Batchelet S., Moritz R.L., Pellett S.,
RA Haugen B.J., Blattner F.R., Welch R.A.;
RT "Uropathogenic Escherichia coli use D-serine deaminase to modulate
RT infection of the murine urinary tract.";
RL Mol. Microbiol. 49:55-67(2003).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=16952954; DOI=10.1128/jb.00634-06;
RA Anfora A.T., Welch R.A.;
RT "DsdX is the second D-serine transporter in uropathogenic Escherichia coli
RT clinical isolate CFT073.";
RL J. Bacteriol. 188:6622-6628(2006).
RN [4]
RP CORRECTION OF DISRUPTION PHENOTYPE.
RX PubMed=26366567; DOI=10.1371/journal.pone.0138121;
RA Hryckowian A.J., Baisa G.A., Schwartz K.J., Welch R.A.;
RT "dsdA does not affect colonization of the murine urinary tract by
RT Escherichia coli CFT073.";
RL PLoS ONE 10:E0138121-E0138121(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:13977,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; EC=4.3.1.18;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01030};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01030};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01030}.
CC -!- DISRUPTION PHENOTYPE: Initially shown to have a 5-6 hour lag phase when
CC grown in human urine, bacteria are initially rounded and swollen but
CC are close to wild-type in morphology by 24 hours and to be more
CC competitive than wild-type in mouse infection (PubMed:12823810). The
CC wild-type (wt) control was later shown to have an amber mutation in
CC rpoS; when the dsdA gene is disrupted in a strain wt for rpoS a growth
CC defect in human urine, lack of growth on minimal medium with D-serine
CC and no difference in growth in a mouse infection model was seen
CC (PubMed:26366567). Single deletion, grows on D-alanine but not D-serine
CC or D-serine plus glycerol (PubMed:16952954).
CC {ECO:0000269|PubMed:12823810, ECO:0000269|PubMed:16952954,
CC ECO:0000269|PubMed:26366567}.
CC -!- MISCELLANEOUS: E.coli CFT073, a uropathogenic strain (UPEC), was
CC originally isolated from urine, which has a high concentration of D-
CC serine. D-serine is toxic to bacteria. The ability to take up D-serine
CC coupled with the activity of this enzyme may allow use of this amino
CC acid as a carbon source in a sugar-poor environment.
CC {ECO:0000305|PubMed:12823810, ECO:0000305|PubMed:16952954}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. DsdA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01030}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014075; AAN81351.1; -; Genomic_DNA.
DR RefSeq; WP_000426391.1; NC_004431.1.
DR AlphaFoldDB; Q8FFF4; -.
DR SMR; Q8FFF4; -.
DR STRING; 199310.c2901; -.
DR EnsemblBacteria; AAN81351; AAN81351; c2901.
DR KEGG; ecc:c2901; -.
DR eggNOG; COG3048; Bacteria.
DR HOGENOM; CLU_035707_0_0_6; -.
DR OMA; ESDPNCF; -.
DR BioCyc; ECOL199310:C2901-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0008721; F:D-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0046416; P:D-amino acid metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_01030; D_Ser_dehydrat; 1.
DR InterPro; IPR011780; D_Ser_am_lyase.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR PANTHER; PTHR48078:SF9; PTHR48078:SF9; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR02035; D_Ser_am_lyase; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Lyase; Pyridoxal phosphate.
FT CHAIN 1..442
FT /note="D-serine dehydratase"
FT /id="PRO_0000185612"
FT MOD_RES 118
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 442 AA; 47829 MW; 6A6837B7A240834A CRC64;
MENAKMNSLI AQYPLVEDLV ALKETTWFNP GTTSLAEGLP YVGLTEQDVQ DAHARLSRFA
PYLAKAFPET AAAGGIIESE LVAIPAMQKR LEKEYQQPIA GQLLLKKDSH LPISGSIKAR
GGIYEVLAHA EKLALEAGLL TLEDDYSKLL SPEFKQFFSQ YSIAVGSTGN LGLSIGIMSA
RIGFKVTVHM SADARAWKKA KLRSHGVTVV EYEQDYGVAV EEGRKAAQSD PNCFFIDDEN
SRTLFLGYSV AGQRLKAQFA QQGRIVDADN PLFVYLPCGV GGGPGGVAFG LKLAFGDHVH
CFFAEPTHSP CMLLGVHTGL HDQISVQDIG IDNLTAADGL AVGRASGFVG RAMERLLDGF
YTLSDQTMYD MLGWLAQEEG IRLEPSALAG MAGSQRVCAS VSYQQMHGFS AEQLRNATHL
VWATGGGMVP EEEMNQYLAK GR
