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Database: UniProt
Entry: Q3AZ44_SYNS9
LinkDB: Q3AZ44_SYNS9
Original site: Q3AZ44_SYNS9 
ID   Q3AZ44_SYNS9            Unreviewed;       491 AA.
AC   Q3AZ44;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:ABB25633.1};
DE            EC=2.5.1.48 {ECO:0000313|EMBL:ABB25633.1};
GN   OrderedLocusNames=Syncc9902_0665 {ECO:0000313|EMBL:ABB25633.1};
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316279 {ECO:0000313|EMBL:ABB25633.1, ECO:0000313|Proteomes:UP000002712};
RN   [1] {ECO:0000313|Proteomes:UP000002712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902 {ECO:0000313|Proteomes:UP000002712};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) 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; CP000097; ABB25633.1; -; Genomic_DNA.
DR   RefSeq; WP_011359477.1; NC_007513.1.
DR   AlphaFoldDB; Q3AZ44; -.
DR   STRING; 316279.Syncc9902_0665; -.
DR   KEGG; sye:Syncc9902_0665; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_011302_1_0_3; -.
DR   OrthoDB; 262490at2; -.
DR   Proteomes; UP000002712; Chromosome.
DR   GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
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; PTHR42699; -; 1.
DR   PANTHER; PTHR42699:SF1; CYSTATHIONINE GAMMA-SYNTHASE-RELATED; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU362118}; Transferase {ECO:0000313|EMBL:ABB25633.1}.
SQ   SEQUENCE   491 AA;  53535 MW;  D108CDD938675EE2 CRC64;
     MSERNLLKEP CWQGSDLGHP LPDHPHAVSM ALPRWRDVIA YEEHEATCRA ALQTIYPRFG
     LHPFLQELAN QVPSDGMGVW PFASRAAAEA AQKHCQRKSP QSSLRLLDQH KISCLCTDAA
     ASAHAKAFWQ HTGLGASSRQ AAIALGHELA PAPHQGEQAR QRVRQRLAEI HHCSEEHISL
     VPAGMAALHA GLEAVQTLRP GRPTLQLGFP YVDVLKQPQV VFHGSELLRT TNLGDIVATL
     DRLDPAAVIV ELPSNPLLRC VDLPAVAELA HARGIPLIAD DTIGTGINLE ALPYADLVFT
     SLTKSFAGRG NVMAGCLLIS PDSQWRSTLL EAIAPRATLS DADAIALEQN SRDVNDRVPR
     LDANCLALAQ KLEKHPAVKR VLHPKDCKNF QALKKRGAGD GCLLSFELHA GERNAQRVFD
     ALRICKGPSL GTSFSLVCPY TQLAHYEELD WAEACGVPAH LLRVSVGLEQ PDELWSRFRE
     ALSHATNPGK V
//
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