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Database: UniProt
Entry: G7G1Z6_9GAMM
LinkDB: G7G1Z6_9GAMM
Original site: G7G1Z6_9GAMM 
ID   G7G1Z6_9GAMM            Unreviewed;       415 AA.
AC   G7G1Z6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:GAA79419.1};
DE            EC=2.5.1.48 {ECO:0000313|EMBL:GAA79419.1};
GN   Name=metB {ECO:0000313|EMBL:GAA79419.1};
GN   ORFNames=P20495_1920 {ECO:0000313|EMBL:GAA79419.1};
OS   Pseudoalteromonas sp. BSi20495.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=386429 {ECO:0000313|EMBL:GAA79419.1, ECO:0000313|Proteomes:UP000003050};
RN   [1] {ECO:0000313|Proteomes:UP000003050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSi20495 {ECO:0000313|Proteomes:UP000003050};
RX   PubMed=22275105; DOI=10.1128/JB.06427-11;
RA   Bian F., Xie B.B., Qin Q.L., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA   Chen X.L., Zhou B.C., Zhang Y.Z.;
RT   "Genome sequences of six Pseudoalteromonas strains isolated from Arctic sea
RT   ice.";
RL   J. Bacteriol. 194:908-909(2012).
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:GAA79419.1}.
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DR   EMBL; BADY01000064; GAA79419.1; -; Genomic_DNA.
DR   RefSeq; WP_008135890.1; NZ_BADY01000064.1.
DR   AlphaFoldDB; G7G1Z6; -.
DR   Proteomes; UP000003050; Unassembled WGS sequence.
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   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   Transferase {ECO:0000313|EMBL:GAA79419.1}.
FT   MOD_RES         198
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   415 AA;  44872 MW;  6EF28768B3D2B265 CRC64;
     MSEKNKATIA VRSGVEADKH HGAVVAPIYL STTYSFADFD TKRQYDYGRS GNPNRDILAE
     TLAELEGGVR GIITATGMAA VHLATQLLNY DDTLVIPHDC YGGSYRLFTS LQKRGLLKLE
     VLDLTKPESL QKILVIKPKL IWIETPSNPV LRLTDIKAVT DIAKQCGALV AADNTFLSPA
     LQNPIKFGVD IVVHSTTKYI NGHSDVVGGA VIAATQEIGD ELAWWANNIG ITGAPFDSYL
     TLRGLRTLNV RLRQHQENAL AIAKYLEESE FVSQVYYPGL ESHPQHELAK AQQLGFGGMV
     SFDIKGDIND AAAFLTSLHN FSLAESLGGV ESLICHPATM THAGMDATAR LEAGVGDTLI
     RVSVGIEDIE DLLADLERVF TLVKPGRKNN TNRLTKGAGT SSGDAKLSAA YPALW
//
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