METB_HERAU
ID METB_HERAU Reviewed; 319 AA.
AC P24601;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Probable cystathionine gamma-synthase;
DE Short=CGS;
DE EC=2.5.1.48;
DE AltName: Full=O-succinylhomoserine (thiol)-lyase;
DE Flags: Fragment;
GN Name=metB;
OS Herpetosiphon aurantiacus (Herpetosiphon giganteus).
OC Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC Herpetosiphon.
OX NCBI_TaxID=65;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HPA2;
RX PubMed=2020544; DOI=10.1093/nar/19.5.1049;
RA Duesterhoeft A., Erdmann D., Kroeger M.;
RT "Stepwise cloning and molecular characterization of the HgiDI restriction-
RT modification system from Herpetosiphon giganteus Hpa2.";
RL Nucleic Acids Res. 19:1049-1056(1991).
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; X55140; CAA38939.1; -; Genomic_DNA.
DR PIR; S14030; S14030.
DR AlphaFoldDB; P24601; -.
DR SMR; P24601; -.
DR PRIDE; P24601; -.
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..>319
FT /note="Probable cystathionine gamma-synthase"
FT /id="PRO_0000114760"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT NON_TER 319
SQ SEQUENCE 319 AA; 34685 MW; 8C7D14992CC7BEBD CRC64;
MDYGFATRAI HAGQDPESVT GAVIVPIYQT STYAQRGVGD HTGYEYSRTD NPTRTALQTC
LAALEEAKHA LVFASGLGAS TTLMLMLKAG DHVICGDDVY GGTYRLFQRV MTEHGLSFDF
IDMADPEAVR AAIKPNTRLI WLETPTNPLL KLAPIAAITR VAREHGIWTI VDNTFASPYN
QRPITLGADM VLHSTTKYIG GHSDVVGGAI MTSNDELYEK LKFLQNAAGA VPGPFDCWLV
LRGVKTLSIR MRDDERNALA IAQFLTEHPG VEKVIYPGLP SHPQHNLARE QMRGFGGMIS
ILLKGGAEAA NAMVSKTKL
