SDHD_RHILW
ID SDHD_RHILW Reviewed; 440 AA.
AC B5ZNC1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Probable 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=Rleg2_1621;
OS Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395492;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2304;
RX PubMed=21304679; DOI=10.4056/sigs.44642;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT WSM2304, an effective microsymbiont of the South American clover Trifolium
RT polymorphum.";
RL Stand. Genomic Sci. 2:66-76(2010).
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 -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. DsdA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01030}.
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DR EMBL; CP001191; ACI54911.1; -; Genomic_DNA.
DR RefSeq; WP_012557571.1; NC_011369.1.
DR AlphaFoldDB; B5ZNC1; -.
DR SMR; B5ZNC1; -.
DR STRING; 395492.Rleg2_1621; -.
DR PRIDE; B5ZNC1; -.
DR EnsemblBacteria; ACI54911; ACI54911; Rleg2_1621.
DR KEGG; rlt:Rleg2_1621; -.
DR eggNOG; COG3048; Bacteria.
DR HOGENOM; CLU_035707_0_0_5; -.
DR OMA; ESDPNCF; -.
DR OrthoDB; 912282at2; -.
DR Proteomes; UP000008330; 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; 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.
PE 3: Inferred from homology;
KW Lyase; Pyridoxal phosphate.
FT CHAIN 1..440
FT /note="Probable D-serine dehydratase"
FT /id="PRO_1000149390"
FT MOD_RES 111
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ SEQUENCE 440 AA; 48178 MW; D03160F95D0D5688 CRC64;
MNTILPADPA RDEVLAGRPT LWVNPSYRKR AIDTSDLPVS RDDVQIARLN WQRLAPLLAE
CFPELKDSDG EIRSELVELK ELREALGYRT REFGNVFIKA DSHLPVAGSI KARGGVYEVF
LFAENLARQN GLLGDGEDIR KLAAEEARSF FSGYTVAVGS TGNLGLSVGI AARALGFKAT
VHMSSDAKAW KVERLRRLGV EVIQHEADYT SAVENARDIA DADPTIYFVD DEQSRHLFLG
YSAAASELAA QLDERGITID EENPLFLYLP CGIGGAPGGV AFGAKAIFGD NVHAFFVEPV
QSPCTLVHMM SGSQELVSVY DVGLTNKTEA DGMAVARMSA FVAKVMREML AGVYTAADDD
LFKLLRMAWI TQRQKLEPSA AAALLGPHFL VHHGEGRRFQ AEQGIEEKMS RATHILWTTG
GSFVPEEQFQ NFLRQAEAVG
