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Database: UniProt
Entry: V5G201_BYSSN
LinkDB: V5G201_BYSSN
Original site: V5G201_BYSSN 
ID   V5G201_BYSSN            Unreviewed;       399 AA.
AC   V5G201;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:GAD98403.1};
GN   ORFNames=PVAR5_7095 {ECO:0000313|EMBL:GAD98403.1};
OS   Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS   variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD98403.1, ECO:0000313|Proteomes:UP000018001};
RN   [1] {ECO:0000313|Proteomes:UP000018001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX   PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA   Oka T., Ekino K., Fukuda K., Nomura Y.;
RT   "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT   spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL   Genome Announc. 2:E0116213-E0116213(2014).
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:GAD98403.1}.
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DR   EMBL; BAUL01000243; GAD98403.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5G201; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   HOGENOM; CLU_018986_3_0_1; -.
DR   InParanoid; V5G201; -.
DR   OrthoDB; 5482552at2759; -.
DR   Proteomes; UP000018001; 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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018001}.
FT   MOD_RES         205
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   399 AA;  44170 MW;  9B2C8DF3D4F6E4F4 CRC64;
     MANHENARPA TLALHADDAL NNVTDVAPPL HLSTTYRYSD NPEDLVPWAD ATDHHIDPKS
     HIYSRFTSPN GTRFETILSA LTNGHALTYS SGLSALHAAL VLFNPRHISI GQNYHGCFGV
     IGLMSRLTGL QQLDIDCPAE QLEEGDVVLL ETPINPHGVA SNIEEYAKKA HSRGAFLIVD
     STFAPPALQD PFLWGADLVM HSGSKYFGGH SDVLCGVLVT QKKAWYDKLL GDRLYLGSVM
     GNMESWLGVR SLRTLEVRVQ RQSQNAEKLV AWLDNAMQAS DPLAGSDEAV AKAALHKVYH
     ASLQKEDMSW LRKQMPNGYG PVFSIILKEE EFARKVPTKL AFFHHATSLG GVESLIEWRT
     MTDAKVDRRL LRISVGLENW EDLKNDLVAA FRAVLQEKA
//
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