ID I1L5U9_SOYBN Unreviewed; 536 AA.
AC I1L5U9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Cystathionine gamma-synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=GLYMA_09G235400 {ECO:0000313|EMBL:KRH40054.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH40054.1};
RN [1] {ECO:0000313|EMBL:KRH40054.1, ECO:0000313|EnsemblPlants:KRH40054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH40054};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH40054.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH40054}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH40054};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH40054.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH40054.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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}.
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DR EMBL; CM000842; KRH40054.1; -; Genomic_DNA.
DR AlphaFoldDB; I1L5U9; -.
DR SMR; I1L5U9; -.
DR STRING; 3847.I1L5U9; -.
DR PaxDb; 3847-GLYMA09G37020-1; -.
DR EnsemblPlants; KRH40054; KRH40054; GLYMA_09G235400.
DR Gramene; KRH40054; KRH40054; GLYMA_09G235400.
DR eggNOG; KOG0053; Eukaryota.
DR HOGENOM; CLU_018986_1_2_1; -.
DR InParanoid; I1L5U9; -.
DR OMA; NAFQIIQ; -.
DR OrthoDB; 6018at2759; -.
DR Proteomes; UP000008827; Chromosome 9.
DR ExpressionAtlas; I1L5U9; baseline and differential.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
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; IPR044639; CGS1/2.
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; PTHR43379; CYSTATHIONINE GAMMA-SYNTHASE; 1.
DR PANTHER; PTHR43379:SF1; CYSTATHIONINE GAMMA-SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 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|RuleBase:RU362118};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT REGION 13..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 58082 MW; 000F83C7F8E35F3A CRC64;
MAVSSSHMRF TFECRSDPDF SPPPPSFDNL RRRNFRSSAG SGAAFHGISS LILRFPPNFQ
RQLSTKARRN CSNIGVAQIV AASWSNNSDN SPAAGAPAPP AATATDAATV PLPVVVAANE
DVVVSAAADE NGAVQLNSSS YSSFLKSDAS KTIHAAERLG RGIETDGITT PVVNTSAYFF
KKTADLIDFK ENRQVSYEYG RYGNPTTVVL EEKISALEGA ESTVIMASGM CASVVLFMAL
VPAGGHLVTT TDCYRKTRIF IETFLPKMGI TTTVIDPADV GALESALEQH NVSLFFTESP
TNPFLRCVDI KLVSELCHKK GTLLCIDGTF ATPLNQKALA LGADLILHSL TKYMGGHHDV
LGGCISGSIK VVSQIRTLHH VLGGTLNPNA AYLFIRGMKT LHLRVQQQNS TGMRMAKLLE
AHPKVKRVYY PGLPSHPEHE LAKRQMTGFG GVVSFEIDGD LHTTIKFIDS LKIPYIAASF
GGCESIVDQP AILSYWDLPQ SERAKYKIYD NLVRFSFGVE DFEDLKADVL QALEAI
//
