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Database: UniProt
Entry: A0A011M9H9_9PROT
LinkDB: A0A011M9H9_9PROT
Original site: A0A011M9H9_9PROT 
ID   A0A011M9H9_9PROT        Unreviewed;       406 AA.
AC   A0A011M9H9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:EXI66373.1};
DE            EC=4.4.1.11 {ECO:0000313|EMBL:EXI66373.1};
GN   Name=mdeA_2 {ECO:0000313|EMBL:EXI66373.1};
GN   ORFNames=AW08_02730 {ECO:0000313|EMBL:EXI66373.1};
OS   Candidatus Accumulibacter adjunctus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI66373.1, ECO:0000313|Proteomes:UP000020218};
RN   [1] {ECO:0000313|EMBL:EXI66373.1, ECO:0000313|Proteomes:UP000020218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-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:EXI66373.1}.
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DR   EMBL; JFAX01000016; EXI66373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A011M9H9; -.
DR   STRING; 1454001.AW08_02730; -.
DR   PATRIC; fig|1454001.3.peg.2779; -.
DR   Proteomes; UP000020218; Unassembled WGS sequence.
DR   GO; GO:0018826; F:methionine gamma-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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:SF15; 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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:EXI66373.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020218}.
FT   MOD_RES         204
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   406 AA;  43972 MW;  5A4481B275FF09E9 CRC64;
     MSFDPASRVQ DYLVFGEFGD VNPSITDSST YTFLSPERME ELFEHEIEGC FLYSRHFNPT
     NKYLASALVR MEDGEAAQVM ASGMGAISTT LMTLCAAGDE IVCGRSIYGG TYALLKNLLP
     RFGVTTRFVD LCNREAVRAA MTPRTRVLYC ESLSNPLLEV SDLPQLAELA HAAGARLVVD
     NTFTPMILSP LRHGADVVVH SLTKFINGTS DCVAGCVVST REFIGQLNDI NSGPSMLFGP
     VLDSARAASI LKNLHSLHIR LRQHGSNALH LATSLTALGY TVHYPGLETH PQHELLARLM
     NPGYGWGGMM TFDAGDHAAA NRLMTLMQRD KVGYLAVSLG YFKTLFTTPG HSTSSEIPFA
     EREAAGLREG LIRFSIGLDA DIAQTTSRIL DCLSEAGISP GSRPAG
//
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