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Database: UniProt
Entry: A0A0U4NF05_9GAMM
LinkDB: A0A0U4NF05_9GAMM
Original site: A0A0U4NF05_9GAMM 
ID   A0A0U4NF05_9GAMM        Unreviewed;       399 AA.
AC   A0A0U4NF05;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:ALZ75103.1};
GN   ORFNames=ATY27_04590 {ECO:0000313|EMBL:ALZ75103.1}, ATY27_12350
GN   {ECO:0000313|EMBL:ALZ76471.1};
OS   Rheinheimera sp. F8.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=1763998 {ECO:0000313|EMBL:ALZ75103.1, ECO:0000313|Proteomes:UP000059499};
RN   [1] {ECO:0000313|Proteomes:UP000059499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F8 {ECO:0000313|Proteomes:UP000059499};
RA   Schuster A.K., Szewzyk U.;
RT   "Draft genome sequence of Rheinheimera sp. F8, a biofilm-forming strain
RT   which produces large amounts of extracellular DNA.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALZ75103.1, ECO:0000313|Proteomes:UP000059499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F8 {ECO:0000313|EMBL:ALZ75103.1,
RC   ECO:0000313|Proteomes:UP000059499};
RX   PubMed=26966195;
RA   Schuster A.K., Szewzyk U.;
RT   "Draft Genome Sequence of Rheinheimera sp. F8, a Biofilm-Forming Strain
RT   Which Produces Large Amounts of Extracellular DNA.";
RL   Genome Announc. 4:0-0(2016).
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}.
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DR   EMBL; CP013656; ALZ75103.1; -; Genomic_DNA.
DR   EMBL; CP013656; ALZ76471.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U4NF05; -.
DR   Proteomes; UP000059499; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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:SF90; CYSTATHIONINE GAMMA-LYASE; 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   Lyase {ECO:0000313|EMBL:ALZ75103.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059499}.
FT   MOD_RES         209
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   399 AA;  43448 MW;  23E9FC2474808922 CRC64;
     MSSSSKHAET MCIHAGKTYD RQFGSLATPL YQTSTFVFDS AEQGAARFAG ETEGYIYTRL
     GNPTTRELEL KVAALEGMAD GAATATGMGA VAAATLAFLQ QGDHLIASNA IYGCSFALFN
     HQFARYGIEV SFVDMTDHAA VEAARRPNTR MLFAETPINP NLVVLDLEFL GRFCRQHQIK
     SVIDNTFLTP LLQQPARYGI DIIIHSATKY LNGHGDVVAG IILSDTDTVQ TIKLTTLKDM
     GATISPHDAW LIIRGLKTLS VRMERHCQNA QRVAEFLQAH PAVATVYYPG LPGHPGHRFI
     GTQMKAAGGV LAFELKGSLD DGRYFINQCE LLSLAVSLGD AESLIQHPAS MTHSPYTAEE
     RRLAGISDGL IRISVGLEHV EDIIADLQQA LVKMQLQQK
//
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