ID   B4FJ26_MAIZE            Unreviewed;       322 AA.
AC   B4FJ26;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Cystathionine gamma-synthase 1 chloroplastic {ECO:0000313|EMBL:ONL98434.1};
GN   ORFNames=ZEAMMB73_Zm00001d029324 {ECO:0000313|EMBL:ONL98434.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ACF82119.1};
RN   [1] {ECO:0000313|EMBL:ACF82119.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B73 {ECO:0000313|EMBL:ACF82119.1};
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [2] {ECO:0000313|EMBL:ONL98434.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONL98434.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) 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; BT037114; ACF82119.1; -; mRNA.
DR   EMBL; BT038485; ACF83490.1; -; mRNA.
DR   EMBL; CM007647; ONL98434.1; -; Genomic_DNA.
DR   EMBL; CM007647; ONL98442.1; -; Genomic_DNA.
DR   EMBL; CM007647; ONL98443.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4FJ26; -.
DR   PaxDb; 4577-GRMZM2G075153_P02; -.
DR   eggNOG; KOG0053; Eukaryota.
DR   HOGENOM; CLU_018986_2_0_1; -.
DR   ExpressionAtlas; B4FJ26; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF6; CYSTATHIONINE GAMMA-SYNTHASE; 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   2: Evidence at transcript level;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   MOD_RES         139
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   322 AA;  35505 MW;  13C0559F80C77A1B CRC64;
     MSALEKAEST VFVASGMYAA VAMLSALVPA GGHIVTTTDC YRKTRIYMEN ELPKRGISMT
     VIRPADMDAL QNALDNNNVS LFFTETPTNP FLRCIDIEHV SNMCHSKGAL LCIDSTFASP
     INQKALTLGA DLVIHSATKY IAGHNDVIGG CVSGRDELVS KVRIYHHVVG GVLNPNAAYL
     ILRGMKTLHL RVQCQNDTAL RMAQFLEEHP KIARVYYPGL PSHPEHHIAK SQMTGFGGVV
     SFEVAGDFDA TRKFIDSVKI PYHAPSFGGC ESIIDQPAIM SYWDSKEQRD IYGIKDNLIR
     FSIGVEDFED LKNDLVQALE KI
//