ID A0A165QVQ6_EXIGL Unreviewed; 404 AA.
AC A0A165QVQ6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 08-NOV-2023, entry version 24.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:KZW04137.1};
GN ORFNames=EXIGLDRAFT_716135 {ECO:0000313|EMBL:KZW04137.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW04137.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZW04137.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZW04137.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV425882; KZW04137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165QVQ6; -.
DR STRING; 1314781.A0A165QVQ6; -.
DR InParanoid; A0A165QVQ6; -.
DR OrthoDB; 5482552at2759; -.
DR Proteomes; UP000077266; 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:UP000077266}.
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 404 AA; 44312 MW; 35D2251E6DDA7BA5 CRC64;
MLKYPVALDL FAAVTMSSGL GTVLLHSDDD PTRAEVAPSI SVTTTFRHSK DVDLKDFDPI
KPHHHVYSRY TQDVTTRVER VLGQLHGEGK HALTFSSGLS AVFTAMVHTA PKRVCVSGGY
FGSHASIAVY GKAAQRTVPL VPLDAKFEPG DVCWLETPVN PTGEARDIQH YADKIHAVGG
KLCVDATFAP PPLSDPFKFG ADIVLHSGTK YFGGHSDLLC GVLVVKSPAE WKELWDIRVY
LGNTMGSFES WLLLRSLRTL HVRVPQQSKT ATALAQWLYK HSQTPRGETW DGVPGGVVHS
VQHASLQTEK FVKEQLPNGF PPTFSVMLHD IAAADEVAFH LHIFTPATSL GGVESLIEQR
FKADGITDRR LLRISVGLEE LEDLKGDLRQ ALRKVADKKA VTKL
//
