ID A7NPM7_ROSCS Unreviewed; 372 AA.
AC A7NPM7;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:ABU59523.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:ABU59523.1};
GN OrderedLocusNames=Rcas_3473 {ECO:0000313|EMBL:ABU59523.1};
OS Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=383372 {ECO:0000313|EMBL:ABU59523.1, ECO:0000313|Proteomes:UP000000263};
RN [1] {ECO:0000313|EMBL:ABU59523.1, ECO:0000313|Proteomes:UP000000263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13941 / HLO8 {ECO:0000313|Proteomes:UP000000263};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|RuleBase:RU362118}.
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DR EMBL; CP000804; ABU59523.1; -; Genomic_DNA.
DR RefSeq; WP_012121946.1; NC_009767.1.
DR AlphaFoldDB; A7NPM7; -.
DR STRING; 383372.Rcas_3473; -.
DR KEGG; rca:Rcas_3473; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_0; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000000263; Chromosome.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
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:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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:SF93; CYSTATHIONINE GAMMA-LYASE-RELATED; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000263};
KW Transferase {ECO:0000313|EMBL:ABU59523.1}.
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 372 AA; 39775 MW; C596420BAA34BCDA CRC64;
MHPETASIHA GQEIDPTTGA VIPPIYLTTT FERASDGSFP RGYIYTRNGN PNRAMLETCL
AALEGGATCV AFSSGLAAAM SVFQALRPGD HVIAPDDAYH GITRLLREIM APWGLEYSRV
DMRDPQNVAA ALRPNTRLVW IETPSNPLLK IADIAAIAEI ARQAGALCAV DNTWATPVQQ
RPLELGADIV MHATTKYIGG HSDVLGGAVV FGANDAFAER VRFLQINGGA VPSPFDCWLA
LRGIQTLPYR VRAHAANAIQ VARFLAEHPR IERVHYPGLE THPGHAVAAR QMRGFGGMLS
IEVEGGEAEA MAVAAKVKII TRATSLGGVE SLIEHRASVE GPESTTPPNL LRISVGLEHP
DDLIADLAQA LT
//
