ID   SDHA_ANAPI              Reviewed;          30 AA.
AC   P80212;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-JUN-2021, entry version 54.
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;
DE   Flags: Fragment;
OS   Anaerotignum propionicum (Clostridium propionicum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerotignum.
OX   NCBI_TaxID=28446;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2;
RX   PubMed=8344301; DOI=10.1111/j.1432-1033.1993.tb18040.x;
RA   Hofmeister A.E.M., Grabowski R., Linder D., Buckel W.;
RT   "L-serine and L-threonine dehydratase from Clostridium propionicum. Two
RT   enzymes with different prosthetic groups.";
RL   Eur. J. Biochem. 215:341-349(1993).
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: Heterodimer of an alpha chain and a beta chain.
CC   -!- SIMILARITY: Belongs to the iron-sulfur dependent L-serine dehydratase
CC       family. {ECO:0000305}.
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   PIR; S34761; S34761.
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.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Gluconeogenesis; Iron; Iron-sulfur;
KW   Lyase; Metal-binding.
FT   CHAIN           1..>30
FT                   /note="L-serine dehydratase, alpha chain"
FT                   /id="PRO_0000171913"
FT   NON_TER         30
SQ   SEQUENCE   30 AA;  3394 MW;  2AA4843780234641 CRC64;
     MKYDSLADLV VQAEKQNVPL XXLIXKDQAE