ID L8DKF1_9NOCA Unreviewed; 390 AA.
AC L8DKF1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:CCQ17371.1};
GN ORFNames=RHODMAR_3985 {ECO:0000313|EMBL:CCQ17371.1};
OS Rhodococcus sp. AW25M09.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1268303 {ECO:0000313|EMBL:CCQ17371.1, ECO:0000313|Proteomes:UP000011207};
RN [1] {ECO:0000313|EMBL:CCQ17371.1, ECO:0000313|Proteomes:UP000011207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AW25M09 {ECO:0000313|EMBL:CCQ17371.1,
RC ECO:0000313|Proteomes:UP000011207};
RA Hjerde E., Pierechod M.M., Williamson A.K., Bjerga G., Willassen N.P.,
RA Smalaas A.O., Altermark B.;
RT "Draft genome sequence of Rhodococcus sp. AW25M09. An Actinomycete isolated
RT from Atlantic Hagfish caught in Hadselfjorden, North- Norway.";
RL Submitted (DEC-2012) 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|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCQ17371.1}.
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DR EMBL; CAPS01000109; CCQ17371.1; -; Genomic_DNA.
DR RefSeq; WP_008718445.1; NZ_CAPS01000109.1.
DR AlphaFoldDB; L8DKF1; -.
DR STRING; 1268303.RHODMAR_3985; -.
DR eggNOG; COG0626; Bacteria.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000011207; Unassembled WGS sequence.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
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; 3.90.1150.10; 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:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 390 AA; 41305 MW; 3DB40CA38F96A9D2 CRC64;
MSEQRSKADN SSWQGFSTKA VHAGYEPDPL TGAVNVPIYA SSTFAQDGVG GMRSGFEYAR
TGNPTRRPLE ANLAALESGH FGRAFSSGMA ATDCALRTIL RPGDHLVIPN DAYGGTFRLI
DKVFTQWGIE YSVAPVSDVD AVRDAIRPNT KLVWVETPTN PLLNVGDIEA LAAVAHEAGT
KMLVDNTFAS PYLQQPLTLG ADIVLHSTTK YIGGHSDVVG GALITNDEEL DTGFAFLQNG
SGGVPGPFDA FLTMRGIKTL ALRMEQHSTN AEKIVEFLDS HPAISQVIYP GLESHPSHAV
AAKQMRRFGG MVSVRLAGGK QAALDFCAKT EIFTLAESLG GVESLIEHPG AMTHASTAGS
LLEVPDDLVR LSVGIEDGAD LVGDVEQALA
//
