ID   SDHL_HELPJ              Reviewed;         455 AA.
AC   Q9ZMU7;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=L-serine dehydratase;
DE            Short=SDH;
DE            EC=4.3.1.17;
DE   AltName: Full=L-serine deaminase;
DE            Short=L-SD;
GN   Name=sdaA; OrderedLocusNames=jhp_0120;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SIMILARITY: Belongs to the iron-sulfur dependent L-serine dehydratase
CC       family. {ECO:0000305}.
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DR   EMBL; AE001439; AAD05697.1; -; Genomic_DNA.
DR   PIR; B71971; B71971.
DR   RefSeq; WP_000135987.1; NC_000921.1.
DR   AlphaFoldDB; Q9ZMU7; -.
DR   SMR; Q9ZMU7; -.
DR   STRING; 85963.jhp_0120; -.
DR   EnsemblBacteria; AAD05697; AAD05697; jhp_0120.
DR   KEGG; hpj:jhp_0120; -.
DR   eggNOG; COG1760; Bacteria.
DR   OMA; SAAMGGC; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000804; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003941; F:L-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1330.90; -; 1.
DR   InterPro; IPR029009; ASB_dom_sf.
DR   InterPro; IPR004644; Fe-S_L-Ser_mono.
DR   InterPro; IPR005130; Ser_deHydtase-like_asu.
DR   InterPro; IPR005131; Ser_deHydtase_bsu.
DR   Pfam; PF03313; SDH_alpha; 1.
DR   Pfam; PF03315; SDH_beta; 1.
DR   SUPFAM; SSF143548; SSF143548; 1.
DR   TIGRFAMs; TIGR00720; sda_mono; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Gluconeogenesis; Iron; Iron-sulfur; Lyase; Metal-binding.
FT   CHAIN           1..455
FT                   /note="L-serine dehydratase"
FT                   /id="PRO_0000171908"
SQ   SEQUENCE   455 AA;  49229 MW;  48248F71BE7C7713 CRC64;
     MASFSILSIF KIGVGPSSSH TIGPMEAGAR FCGLLKGILE QVERVQITLH GSLALTGKGH
     LSDEAVLIGL HGIYANELDI TTKKALLHEA FENKVLKLAN QHHIPFDYAK DLIFDNKPLA
     RHQNALILKA FNAKNEVLKE ETYYSVGGGF VYTEKELDNL SEEGENESVA YDFSSAKELL
     ELCQKHQKSI AEIVRLRENA LKNHPDATMT KIYHAMLECY HNGANSKERY LPGSLKVTRL
     APSVKTRLEK HPTSGKDPLA LIDYISLYAR SIAEENASGG KVVTAPTNGA CAVVPSVLSY
     AKNHLFENLS QKSINDFLLT SAAIGYLYKK NASLSGAEAG CQAEIGVASS MAAGGLAHLC
     QATTQQVLIA SEIAMEHHLG LTCDPVGGLV QIPCIERNVL GAIKAISASK LALEDEYKPK
     VSLDEVIATM YATGKDMNEK YKETSLGGLA KTLKC