ID Q2H5Y9_CHAGB Unreviewed; 427 AA.
AC Q2H5Y9;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Cystathionine gamma-synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CHGG_05926 {ECO:0000313|EMBL:EAQ89307.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ89307.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408031; EAQ89307.1; -; Genomic_DNA.
DR RefSeq; XP_001222021.1; XM_001222020.1.
DR AlphaFoldDB; Q2H5Y9; -.
DR STRING; 306901.Q2H5Y9; -.
DR GeneID; 4390994; -.
DR VEuPathDB; FungiDB:CHGG_05926; -.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_3_0_1; -.
DR InParanoid; Q2H5Y9; -.
DR OMA; TFRYPRN; -.
DR OrthoDB; 5482552at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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:SF35; CYSTATHIONINE GAMMA-SYNTHASE (AFU_ORTHOLOGUE AFUA_7G01590); 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:UP000001056}.
FT MOD_RES 226
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 427 AA; 47317 MW; E36A8B8BDA01E77D CRC64;
MVSNGNTEKK AAGAGPDQLA AAFGRQLSLA SRSVHADDYT NTHTAVAPPM HVSTTFRYPR
NPDELVAWSD VEPEKWDDFY IYSREKSPNT TRYEAILSSI LGGPAVSYAS GLAAFHAMVV
FLNPKRVAIG GGYHGCHGIL KLMNKLNGLE QLELENEDDL AKLQKGDIIH VETPLNPTGE
ARDLAYYRKK ADELGCYLTV DATFAPPPLQ DPFKYGVDII MHSGTKYFGG HSDMLSGVLA
IHPDRAGSKD GKPGWLTEIR EERLHLGGVM GSFEGWLGTR SLRTLELRVK RQSETTRNLV
DWLASQKKAG GNVVADLVYK LQHSSQQPEA SDPDSWLSKQ MPNGHGPVFS LWLQSEELAK
RLPSKLFLFH HATSLGGIES LVEWRAMSDT TVDRRLVRVS IGVESWEDLR DDLLQGFQAL
HKELNNN
//