ID H0JW80_9NOCA Unreviewed; 383 AA.
AC H0JW80;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:EHK81631.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:EHK81631.1};
GN ORFNames=AK37_19773 {ECO:0000313|EMBL:EHK81631.1};
OS Rhodococcus pyridinivorans AK37.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1114960 {ECO:0000313|EMBL:EHK81631.1, ECO:0000313|Proteomes:UP000005064};
RN [1] {ECO:0000313|EMBL:EHK81631.1, ECO:0000313|Proteomes:UP000005064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK37 {ECO:0000313|EMBL:EHK81631.1,
RC ECO:0000313|Proteomes:UP000005064};
RA Kriszt B., Tancsics A., Cserhati M., Toth A., Nagy I., Horvath B.,
RA Tamura T., Kukolya J., Szoboszlay S.;
RL Submitted (DEC-2011) 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:EHK81631.1}.
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DR EMBL; AHBW01000054; EHK81631.1; -; Genomic_DNA.
DR RefSeq; WP_006553875.1; NZ_AHBW01000054.1.
DR AlphaFoldDB; H0JW80; -.
DR PATRIC; fig|1114960.4.peg.4033; -.
DR Proteomes; UP000005064; Unassembled WGS sequence.
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: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};
KW Transferase {ECO:0000313|EMBL:EHK81631.1}.
FT MOD_RES 203
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 383 AA; 40786 MW; 18C2BF56446A94B0 CRC64;
MTDQNQHGFA TRAIHAGYEP DPQTGAVNVP IYASSTFAQD GVGEMRNGFE YARTGNPTRR
PLEANLAALE NGTYGRAFGS GMAATDCLLR SVLRPGDHLV IPNDAYGGTF RLIDKVFTQW
GIEYTPAAIN DADEVRAAVR PNTKLVWVET PTNPLLNIGD ISALADIAHE GGARLVVDNT
FASPYLQQPL TFGADVVLHS TTKYIGGHSD VVGGALVTND EELDAAFAFL QNGAGAVPGP
FDAFLTLRGI KTLAVRMEKH SDNAEKLVDF LSGHSAVTKV LYPGLESHPG HEYAAKQMRR
FGGMISVRLA GGRQAALDFC KRTEIFTLAE SLGGVESLIE HPGAMTHAST AGSLLEVPED
LVRLSVGIED AADLLADVEQ ALG
//
