ID   SDHB_PEPAS              Reviewed;         222 AA.
AC   P33074;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=L-serine dehydratase, beta chain;
DE            Short=SDH;
DE            EC=4.3.1.17;
DE   AltName: Full=L-serine deaminase;
DE            Short=L-SD;
GN   Name=sdhB;
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 4-19.
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}.
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; U76260; AAC45545.1; -; Genomic_DNA.
DR   PIR; S16376; S16376.
DR   AlphaFoldDB; P33074; -.
DR   SMR; P33074; -.
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   Gene3D; 3.30.1330.90; -; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR029009; ASB_dom_sf.
DR   InterPro; IPR004643; Fe-S_L-Ser_bsu.
DR   InterPro; IPR005131; Ser_deHydtase_bsu.
DR   Pfam; PF03315; SDH_beta; 1.
DR   PIRSF; PIRSF036692; SDH_B; 1.
DR   SUPFAM; SSF143548; SSF143548; 1.
DR   SUPFAM; SSF55021; SSF55021; 1.
DR   TIGRFAMs; TIGR00719; sda_beta; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Gluconeogenesis; Iron; Iron-sulfur;
KW   Lyase; Metal-binding.
FT   CHAIN           1..222
FT                   /note="L-serine dehydratase, beta chain"
FT                   /id="PRO_0000171918"
FT   DOMAIN          150..222
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
SQ   SEQUENCE   222 AA;  24151 MW;  3A2A624EC3104C08 CRC64;
     MTDYSAFEVM GPIMVGPSSS HTAGACKIAN VATSIVSNNY NQVEFQLHGS FAHTFKGHGT
     DRALVGGILG FEPDDDRIKT SFELAKQAGL NYIFTTTNLG DNYHPNSVKI VFSYPNGEEE
     YVIGSSIGGG AMKIVNINGI AIEFRGEYST ILLEYPEQRG VISYVSSLLT GSEYNIESLN
     TKKNKLTNIV TLTVEIDKPL TESLKSAILG VERFTTAKYV EV