ID   Y1077_MYCTO             Reviewed;         464 AA.
AC   P9WP50; L0T8D3; Q79FT1; Q7D8W0;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Putative cystathionine beta-synthase MT1108;
DE            EC=4.2.1.22;
DE   AltName: Full=Beta-thionase;
DE   AltName: Full=Serine sulfhydrase;
GN   Name=cbs; OrderedLocusNames=MT1108;
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-homocysteine + L-serine = H2O + L,L-cystathionine;
CC         Xref=Rhea:RHEA:10112, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:58161, ChEBI:CHEBI:58199; EC=4.2.1.22;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45364.1; -; Genomic_DNA.
DR   PIR; C70894; C70894.
DR   RefSeq; WP_003405730.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WP50; -.
DR   SMR; P9WP50; -.
DR   EnsemblBacteria; AAK45364; AAK45364; MT1108.
DR   GeneID; 45425049; -.
DR   KEGG; mtc:MT1108; -.
DR   PATRIC; fig|83331.31.peg.1193; -.
DR   HOGENOM; CLU_021018_0_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004122; F:cystathionine beta-synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IEA:InterPro.
DR   CDD; cd04608; CBS_pair_CBS; 1.
DR   Gene3D; 3.10.580.10; -; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR046353; CBS_C.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR005857; Cysta_beta_synth.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF00291; PALP; 1.
DR   SMART; SM00116; CBS; 2.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   TIGRFAMs; TIGR01137; cysta_beta; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate.
FT   CHAIN           1..464
FT                   /note="Putative cystathionine beta-synthase MT1108"
FT                   /id="PRO_0000427013"
FT   BINDING         74
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         44
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   464 AA;  48635 MW;  BF53318ECB10BB81 CRC64;
     MRIAQHISEL IGGTPLVRLN SVVPDGAGTV AAKVEYLNPG GSSKDRIAVK MIEAAEASGQ
     LKPGGTIVEP TSGNTGVGLA LVAQRRGYKC VFVCPDKVSE DKRNVLIAYG AEVVVCPTAV
     PPHDPASYYS VSDRLVRDID GAWKPDQYAN PEGPASHYVT TGPEIWADTE GKVTHFVAGI
     GTGGTITGAG RYLKEVSGGR VRIVGADPEG SVYSGGAGRP YLVEGVGEDF WPAAYDPSVP
     DEIIAVSDSD SFDMTRRLAR EEAMLVGGSC GMAVVAALKV AEEAGPDALI VVLLPDGGRG
     YMSKIFNDAW MSSYGFLRSR LDGSTEQSTV GDVLRRKSGA LPALVHTHPS ETVRDAIGIL
     REYGVSQMPV VGAEPPVMAG EVAGSVSERE LLSAVFEGRA KLADAVSAHM SPPLRMIGAG
     ELVSAAGKAL RDWDALMVVE EGKPVGVITR YDLLGFLSEG AGRR