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Database: UniProt
Entry: A0A071LPX6_9ENTR
LinkDB: A0A071LPX6_9ENTR
Original site: A0A071LPX6_9ENTR 
ID   A0A071LPX6_9ENTR        Unreviewed;       386 AA.
AC   A0A071LPX6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:KEA50355.1};
DE            EC=2.5.1.48 {ECO:0000313|EMBL:KEA50355.1};
GN   ORFNames=DT73_24240 {ECO:0000313|EMBL:KEA50355.1};
OS   Mangrovibacter sp. MFB070.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Mangrovibacter.
OX   NCBI_TaxID=1224318 {ECO:0000313|EMBL:KEA50355.1, ECO:0000313|Proteomes:UP000027726};
RN   [1] {ECO:0000313|EMBL:KEA50355.1, ECO:0000313|Proteomes:UP000027726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MFB070 {ECO:0000313|EMBL:KEA50355.1,
RC   ECO:0000313|Proteomes:UP000027726};
RA   Joseph T.C., Varghese A.M., Baby A., Reghunathan D., V M., Lalitha K.V.;
RT   "Draft Genome Sequence of Mangrovibacter spp. MFB070 a Nitrogen-fixing
RT   Bacterium Isolated from an Aquaculture Farm.";
RL   Submitted (APR-2014) 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:KEA50355.1}.
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DR   EMBL; JJMI01000052; KEA50355.1; -; Genomic_DNA.
DR   RefSeq; WP_036115855.1; NZ_JJMI01000052.1.
DR   AlphaFoldDB; A0A071LPX6; -.
DR   eggNOG; COG0626; Bacteria.
DR   Proteomes; UP000027726; 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   Reference proteome {ECO:0000313|Proteomes:UP000027726};
KW   Transferase {ECO:0000313|EMBL:KEA50355.1}.
FT   MOD_RES         198
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   386 AA;  41490 MW;  7804C56D45A98A30 CRC64;
     MTRKQATIAV RSGLNNDEQY GCVVPPIHLS TTYNFTDFNS PREHDYSRRG NPTRDVVQRT
     LAELEGGAGA VMTNTGMSAI HLLTAIFLNP GDLLVAPHDC YGGSYRLFDS MAKRGCYRVQ
     FVDQNDEAAL ESALAQNPKL VLIESPSNPL LRVVDIAKIC QAAKAAGAIT VVDNTFLSPA
     LQNPLALGAD LVVHSCTKYL NGHSDVVAGA VIAKDADMAT ELAWWANNIG VTGSAFDSYL
     LLRGIRTLAP RVELAQRNAL AIVDYLKKQP LVKRLYHPSL PENPGHDIAV RQQKGFGAML
     SFELDGDEQT LRRFLKGLSL FTLAESLGGV ESLISHAATM THAGMSAEAR AAAGISETLL
     RISTGIEDGD DLIADLENGF RAASEG
//
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