METB_HELPJ
ID METB_HELPJ Reviewed; 380 AA.
AC Q9ZMW7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Cystathionine gamma-synthase;
DE Short=CGS;
DE EC=2.5.1.48;
DE AltName: Full=O-succinylhomoserine (thiol)-lyase;
GN Name=metB; OrderedLocusNames=jhp_0098;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
CC -!- FUNCTION: Catalyzes the formation of L-cystathionine from O-succinyl-L-
CC homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In
CC the absence of thiol, catalyzes gamma-elimination to form 2-
CC oxobutanoate, succinate and ammonia (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine + O-succinyl-L-homoserine = H(+) + L,L-
CC cystathionine + succinate; Xref=Rhea:RHEA:20397, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:35235, ChEBI:CHEBI:57661,
CC ChEBI:CHEBI:58161; EC=2.5.1.48;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000305}.
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DR EMBL; AE001439; AAD05677.1; -; Genomic_DNA.
DR PIR; D71973; D71973.
DR RefSeq; WP_001242773.1; NC_000921.1.
DR AlphaFoldDB; Q9ZMW7; -.
DR SMR; Q9ZMW7; -.
DR STRING; 85963.jhp_0098; -.
DR EnsemblBacteria; AAD05677; AAD05677; jhp_0098.
DR KEGG; hpj:jhp_0098; -.
DR eggNOG; COG0626; Bacteria.
DR OMA; MQTKLIH; -.
DR Proteomes; UP000000804; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808; PTHR11808; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Methionine biosynthesis;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..380
FT /note="Cystathionine gamma-synthase"
FT /id="PRO_0000114759"
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 380 AA; 41223 MW; 358BEAE6C5C802BA CRC64;
MRMQTKLIHG GINEDATTGA VSVPIYQTST YRQDAIGRHK GYEYSRSGNP TRFALEELIA
DLEGGVKGFA FASGLAGIHA VFSLLQSGDH VLLGDDVYGG NFRLFNKVLV KNGLSCTIID
TSDLSQIKKA IKPNTKALYL ETPSNPLLKI TDLAQCASVA KEHNLLTIVD NTFATPYCQN
PLLLGTDIVA HNGTKYLGGH SDVVAGLVTT NNEALAQEFD FFQNAIGGVL GLQDSWLLQR
GIKTLGLRME AHQKNALCVA EFLEKHPKVE RVYYPGLPTH PNHELAKAQM RGFSGMFSFT
LKNDSEAVAF VESLKLFILG ESLGGVESLV GIPALMTHAC IPKAQREAAG IRDGLVRLSV
GIEHEQDLLE DLDQAFAKIS