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Database: UniProt
Entry: A0A081NX44_9BACL
LinkDB: A0A081NX44_9BACL
Original site: A0A081NX44_9BACL 
ID   A0A081NX44_9BACL        Unreviewed;       399 AA.
AC   A0A081NX44;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:KEQ23017.1};
DE            EC=2.5.1.48 {ECO:0000313|EMBL:KEQ23017.1};
GN   ORFNames=ET33_19055 {ECO:0000313|EMBL:KEQ23017.1};
OS   Paenibacillus tyrfis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1501230 {ECO:0000313|EMBL:KEQ23017.1, ECO:0000313|Proteomes:UP000028123};
RN   [1] {ECO:0000313|EMBL:KEQ23017.1, ECO:0000313|Proteomes:UP000028123}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSt1 {ECO:0000313|EMBL:KEQ23017.1,
RC   ECO:0000313|Proteomes:UP000028123};
RA   Aw Y.K., Ong K.S., Gan H.M., Lee S.M.;
RT   "Draft genome sequence of Paenibacillus sp. MSt1.";
RL   Submitted (JUN-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:KEQ23017.1}.
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DR   EMBL; JNVM01000028; KEQ23017.1; -; Genomic_DNA.
DR   RefSeq; WP_036689894.1; NZ_JNVM01000028.1.
DR   AlphaFoldDB; A0A081NX44; -.
DR   eggNOG; COG0626; Bacteria.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000028123; 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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11808:SF91; 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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028123};
KW   Transferase {ECO:0000313|EMBL:KEQ23017.1}.
FT   MOD_RES         203
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   399 AA;  43539 MW;  D1DC856717D20579 CRC64;
     MSNCSKPELK IESRLAQIGS QEEPVTGAVS FPVYQATAFR HPKLGQSTGF DYARTKSPTR
     KILEDAIAEL ESGDAGFACS SGMAALQTIF ALFSQGDHLL VSLDLYGGTY RMLERIMSRF
     GVTATYVDTN DLDALEANLQ PGTKAVLIET PTNPLMMVTD LALVCGWAKK KGLLSIVDNT
     LLTPFFQRPI ELGADIVIHS ASKYLGGHND VLAGLIVTKG KELSEEMAFL HNSIGAVLGP
     QDSWLLMRGM KTLAIRMERH EYNATRIATF LQSHPQVEAV YYPALESHPG HDIQKKQSSG
     NTGIFSFKLK DARYIEPILR HVKLIAFAES LGGVESLMTY PAVQTHADIP EDIRSKVGVD
     DKLLRYSVGI EHADDLIADL ARAIDLAQQE IEGGVPAHG
//
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