METB_HELPY
ID METB_HELPY Reviewed; 380 AA.
AC P56069;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=HP_0106;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD07176.1; -; Genomic_DNA.
DR PIR; B64533; B64533.
DR RefSeq; NP_206906.1; NC_000915.1.
DR RefSeq; WP_001242837.1; NC_018939.1.
DR PDB; 4L0O; X-ray; 2.76 A; A/C/E/G/H/K/M/O=1-380.
DR PDBsum; 4L0O; -.
DR AlphaFoldDB; P56069; -.
DR SMR; P56069; -.
DR IntAct; P56069; 1.
DR STRING; 85962.C694_00525; -.
DR PaxDb; P56069; -.
DR EnsemblBacteria; AAD07176; AAD07176; HP_0106.
DR KEGG; hpy:HP_0106; -.
DR PATRIC; fig|85962.47.peg.115; -.
DR eggNOG; COG0626; Bacteria.
DR OMA; MQTKLIH; -.
DR PhylomeDB; P56069; -.
DR BioCyc; MetaCyc:HP_RS00540-MON; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IBA:GO_Central.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IBA:GO_Central.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IBA:GO_Central.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IBA:GO_Central.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Methionine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..380
FT /note="Cystathionine gamma-synthase"
FT /id="PRO_0000114758"
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:4L0O"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:4L0O"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:4L0O"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:4L0O"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:4L0O"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:4L0O"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:4L0O"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:4L0O"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:4L0O"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:4L0O"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:4L0O"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:4L0O"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:4L0O"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:4L0O"
FT HELIX 153..161
FT /evidence="ECO:0007829|PDB:4L0O"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:4L0O"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:4L0O"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:4L0O"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:4L0O"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:4L0O"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:4L0O"
FT TURN 193..198
FT /evidence="ECO:0007829|PDB:4L0O"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:4L0O"
FT HELIX 213..226
FT /evidence="ECO:0007829|PDB:4L0O"
FT HELIX 232..242
FT /evidence="ECO:0007829|PDB:4L0O"
FT HELIX 245..264
FT /evidence="ECO:0007829|PDB:4L0O"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:4L0O"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:4L0O"
FT STRAND 295..303
FT /evidence="ECO:0007829|PDB:4L0O"
FT HELIX 306..312
FT /evidence="ECO:0007829|PDB:4L0O"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:4L0O"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:4L0O"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:4L0O"
FT TURN 333..340
FT /evidence="ECO:0007829|PDB:4L0O"
FT HELIX 343..348
FT /evidence="ECO:0007829|PDB:4L0O"
FT STRAND 355..359
FT /evidence="ECO:0007829|PDB:4L0O"
FT HELIX 365..377
FT /evidence="ECO:0007829|PDB:4L0O"
SQ SEQUENCE 380 AA; 41118 MW; 58A85489B05257ED CRC64;
MRMQTKLIHG GISEDATTGA VSVPIYQTST YRQDAIGRHK GYEYSRSGNP TRFALEELIA
DLEGGVKGFA FASGLAGIHA VFSLLQSGDH VLLGDDVYGG TFRLFNQVLV KNGLSCTIID
TSDISQIKKA IKPNTKALYL ETPSNPLLKI TDLAQCASVA KDHGLLTIVD NTFATPYYQN
PLLLGADIVA HSGTKYLGGH SDVVAGLVTT NNEALAQEIA FFQNAIGGVL GPQDSWLLQR
GIKTLGLRME AHQKNALCVA EFLEKHPKVE RVYYPGLPTH PNYELAKKQM RGFSGMLSFT
LKNDSEAVAF VESLKLFILG ESLGGVESLV GIPAFMTHAC IPKTQREAAG IRDGLVRLSV
GIEHEQDLLE DLEQAFAKIG
