ID A0A094EFP4_9PEZI Unreviewed; 425 AA.
AC A0A094EFP4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 28.
DE RecName: Full=Cystathionine gamma-synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=V499_04765 {ECO:0000313|EMBL:KFY75253.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY75253.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY75253.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY75253.1,
RC ECO:0000313|Proteomes:UP000029295};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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}.
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:KFY75253.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPKB01000726; KFY75253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EFP4; -.
DR HOGENOM; CLU_018986_3_0_1; -.
DR Proteomes; UP000029295; 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}.
FT MOD_RES 216
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 425 AA; 46249 MW; 7234C35E298650EB CRC64;
MSDIKESNVV VPEAASNLSV SSLAIHADDV LNGRHQDVAP PMHVSTTYRY PSDPEKLVPW
TEADHTAAAE GHIYSRHTAP NTTRFETILS SLLNGPAISY SSGLSAFHAI LVHLNPKRIS
IGEGYHGCHG VISIHKKLTG LTTLPLDCPA EDLQPGDIVH IETPLNPTGN ATNLKEYADK
AHSRGAYLTV DATFGPPPLQ DPFLWGADIV MHSGTKYFGG HSDMLCGVLA VNPARVKEGW
VDNLIHERLL IGSVMGNMEG WLGVRSLRTL EIRVERQSLN TGKLVAWLNA ALHPESESSV
GDSATLSSGN SSAIREVLAK VEHASLQTAD IKDGWLLKQM PNGFGPVFSI VMQKEELARR
LPSKLKLFHH ATSLGGVESL IEWRTMTDAT VDRRLLRVSI GLEGWEDLRD DLLQAFTALA
AEQKS
//