ID   SDHA_PEPAS              Reviewed;         292 AA.
AC   P33073; O33922;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=L-serine dehydratase, alpha chain;
DE            Short=SDH;
DE            EC=4.3.1.17;
DE   AltName: Full=L-serine deaminase;
DE            Short=L-SD;
GN   Name=sdhA;
OS   Peptoniphilus asaccharolyticus (Peptostreptococcus asaccharolyticus).
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Peptoniphilus.
OX   NCBI_TaxID=1258;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 14963 / DSM 20463 / JCM 1765 / NCIMB 10074 / NCTC 11461 / UW
RC   228;
RX   PubMed=9244285; DOI=10.1128/jb.179.15.4937-4941.1997;
RA   Hofmeister A.E., Textor S., Buckel W.;
RT   "Cloning and expression of the two genes coding for L-serine dehydratase
RT   from Peptostreptococcus asaccharolyticus: relationship of the iron-sulfur
RT   protein to both L-serine dehydratases from Escherichia coli.";
RL   J. Bacteriol. 179:4937-4941(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-23.
RC   STRAIN=ATCC 14963 / DSM 20463 / JCM 1765 / NCIMB 10074 / NCTC 11461 / UW
RC   228;
RX   PubMed=2065681; DOI=10.1111/j.1432-1033.1991.tb16095.x;
RA   Grabowski R., Buckel W.;
RT   "Purification and properties of an iron-sulfur-containing and pyridoxal-
RT   phosphate-independent L-serine dehydratase from Peptostreptococcus
RT   asaccharolyticus.";
RL   Eur. J. Biochem. 199:89-94(1991).
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;
CC       Note=Binds 1 [4Fe-4S] cluster.;
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Heterooctamer of four alpha chains and four beta chains.
CC   -!- SIMILARITY: Belongs to the iron-sulfur dependent L-serine dehydratase
CC       family. {ECO:0000305}.
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DR   EMBL; U76260; AAC45546.1; -; Genomic_DNA.
DR   PIR; S16224; S16224.
DR   AlphaFoldDB; P33073; -.
DR   SMR; P33073; -.
DR   UniPathway; UPA00138; -.
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   InterPro; IPR005130; Ser_deHydtase-like_asu.
DR   InterPro; IPR004642; Ser_deHydtase_asu.
DR   Pfam; PF03313; SDH_alpha; 1.
DR   TIGRFAMs; TIGR00718; sda_alpha; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Gluconeogenesis; Iron; Iron-sulfur;
KW   Lyase; Metal-binding.
FT   CHAIN           1..292
FT                   /note="L-serine dehydratase, alpha chain"
FT                   /id="PRO_0000171915"
FT   CONFLICT        6
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        12
FT                   /note="C -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   292 AA;  30770 MW;  4247702EEC932AE0 CRC64;
     MLNTAREIID VCNERGIKIY DLVLEEEIKN SHTTEEEIRK KLDAVIDVMH ASATKNLTQS
     DVTEYKMIDG FAKRTYEYAN SGKSIVGDFL AKAMAMAFST SEVNASMGKI VAAPTAGSSG
     IMPAMLVAAT EKYNFDRTTI QNGFLTSIGI GQVITKYATF AGAEGGCQAE CGSASAMAAA
     ALVEMLGGTV EQALHAASIT IINVLGLVCD PIAGLVQYPC TFRNASGVIN AFISADLALA
     GVESLVPFDE VVIAMGEVGN SMIEALRETG LGGLAGSKTG QKIRRDFLKE GD