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Database: UniProt
Entry: A3SR24_ROSNI
LinkDB: A3SR24_ROSNI
Original site: A3SR24_ROSNI 
ID   A3SR24_ROSNI            Unreviewed;       386 AA.
AC   A3SR24;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:EAP75047.1};
GN   ORFNames=ISM_10685 {ECO:0000313|EMBL:EAP75047.1};
OS   Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=89187 {ECO:0000313|EMBL:EAP75047.1, ECO:0000313|Proteomes:UP000005954};
RN   [1] {ECO:0000313|EMBL:EAP75047.1, ECO:0000313|Proteomes:UP000005954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-591 / DSM 15170 / ISM
RC   {ECO:0000313|Proteomes:UP000005954};
RA   Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (DEC-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}.
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:EAP75047.1}.
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DR   EMBL; AALY01000004; EAP75047.1; -; Genomic_DNA.
DR   RefSeq; WP_009814146.1; NZ_CH724156.1.
DR   AlphaFoldDB; A3SR24; -.
DR   STRING; 89187.ISM_10685; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_2_5; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000005954; Unassembled WGS sequence.
DR   GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
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:SF93; CYSTATHIONINE GAMMA-LYASE-RELATED; 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:UP000005954}.
FT   MOD_RES         205
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   386 AA;  42768 MW;  D1122258C3E4C0C0 CRC64;
     MSDRRNRPLS PSTKLAQALR YLDRETGAIV PPIQPSATYA RDEDYAVRRS YMYRRDGNPT
     TEQAEAIIAD LEGAVDCMLF SSGMSACMSV IDTLKPGDHV VVPEVMYHGV LQQFQRYAKL
     HRLEVSYYRP GDLDALRDAC RKGKTRLVWV ESPNNPDWDV TDIAAAAELA HAAGAKLLTD
     CTGTPPCATR ALELGADFSF HSATKYLNGH SDVTAGALSV RNMDAWWEEI EGHRKLQGTV
     LQSFDAFLLI RGMRTLTLRY ERATLNALRI ATHFEGHPQV RKVLYPGLES HPDHDIAKRQ
     THGMYGGMMS IIVKGDEQAA IDVARFCQLF YPATSLGGVE SLIEHRKTVS GEGFKVHPAL
     LRLSIGIEDA DDLIADLEQA LDRALG
//
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