ID   SDHL_MYCTO              Reviewed;         461 AA.
AC   P9WGT4; L0T5F2; O53614; P66773;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 34.
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=MT0075;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
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; AE000516; AAK44299.1; -; Genomic_DNA.
DR   PIR; F70848; F70848.
DR   RefSeq; WP_003400600.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WGT4; -.
DR   SMR; P9WGT4; -.
DR   EnsemblBacteria; AAK44299; AAK44299; MT0075.
DR   GeneID; 45424031; -.
DR   KEGG; mtc:MT0075; -.
DR   PATRIC; fig|83331.31.peg.78; -.
DR   HOGENOM; CLU_022305_0_1_11; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001020; 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..461
FT                   /note="L-serine dehydratase"
FT                   /id="PRO_0000428306"
SQ   SEQUENCE   461 AA;  48576 MW;  228C62DCE67FEAFD CRC64;
     MTISVFDLFT IGIGPSSSHT VGPMRAANQF VVALRRRGHL DDLEAMRVDL FGSLAATGAG
     HGTMSAILLG LEGCQPETIT TEHKERRLAE IAASGVTRIG GVIPVPLTER DIDLHPDIVL
     PTHPNGMTFT AAGPHGRVLA TETYFSVGGG FIVTEQTSGN SGQHPCSVAL PYVSAQELLD
     ICDRLDVSIS EAALRNETCC RTENEVRAAL LHLRDVMVEC EQRSIAREGL LPGGLRVRRR
     AKVWYDRLNA EDPTRKPEFA EDWVNLVALA VNEENASGGR VVTAPTNGAA GIVPAVLHYA
     IHYTSAGAGD PDDVTVRFLL TAGAIGSLFK ERASISGAEV GCQGEVGSAA AMAAAGLAEI
     LGGTPRQVEN AAEIAMEHSL GLTCDPIAGL VQIPCIERNA ISAGKAINAA RMALRGDGIH
     RVTLDQVIDT MRATGADMHT KYKETSAGGL AINVAVNIVE C