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Database: UniProt
Entry: W7QRN3_9ALTE
LinkDB: W7QRN3_9ALTE
Original site: W7QRN3_9ALTE 
ID   W7QRN3_9ALTE            Unreviewed;       383 AA.
AC   W7QRN3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:EWH11657.1};
GN   ORFNames=DS2_02490 {ECO:0000313|EMBL:EWH11657.1};
OS   Catenovulum agarivorans DS-2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Catenovulum.
OX   NCBI_TaxID=1328313 {ECO:0000313|EMBL:EWH11657.1, ECO:0000313|Proteomes:UP000019276};
RN   [1] {ECO:0000313|EMBL:EWH11657.1, ECO:0000313|Proteomes:UP000019276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-2 {ECO:0000313|EMBL:EWH11657.1,
RC   ECO:0000313|Proteomes:UP000019276};
RX   PubMed=24604650;
RA   Shan D., Li X., Gu Z., Wei G., Gao Z., Shao Z.;
RT   "Draft Genome Sequence of the Agar-Degrading Bacterium Catenovulum sp.
RT   Strain DS-2, Isolated from Intestines of Haliotis diversicolor.";
RL   Genome Announc. 2:e00144-14(2014).
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:EWH11657.1}.
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DR   EMBL; ARZY01000003; EWH11657.1; -; Genomic_DNA.
DR   RefSeq; WP_035013064.1; NZ_ARZY01000003.1.
DR   AlphaFoldDB; W7QRN3; -.
DR   STRING; 1328313.DS2_02490; -.
DR   PATRIC; fig|1328313.3.peg.519; -.
DR   eggNOG; COG0626; Bacteria.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000019276; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; 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; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR011821; O_succ_thio_ly.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR02080; O_succ_thio_ly; 1.
DR   PANTHER; PTHR11808:SF75; CYSTATHIONINE GAMMA-SYNTHASE; 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:UP000019276}.
FT   MOD_RES         198
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   383 AA;  41618 MW;  19F092EA09898DC9 CRC64;
     MSKKNLATIA VRGGIESDGQ YNAVVPPIYL SSTYAFEGFD QKGPYDYSRC GNPSRDILAN
     TLAELEHGAH GVVTATGTAA IHLVCQLLRP DDLLVVPHDC YGGSYRLFVN LAQRGAFKLQ
     VINQTNQQEL DAAFAAKPKV IWVETPSNPL LRITDLADIC NRAKQTETLV AVDNTFLSPV
     FQQPLTLGAD IVVHSTTKYI NGHSDVVGGV VVTKTKELGE ELAWWANCIG ITGSAFDSYM
     TLRGVRTLVP RMKQHQENSL ALVDVLKDHP AVDKVYHPSL PSHPGHEIAK KQQHGFGAML
     SFELKGTTDE VTRFIDKLEH FSLAESLGGT ESLVCHPSTM THAAMDEAAQ LKAGITQTLV
     RFSVGIEDSS ELVADVKQAL DAL
//
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