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Database: UniProt
Entry: A0A011NQP2_9PROT
LinkDB: A0A011NQP2_9PROT
Original site: A0A011NQP2_9PROT 
ID   A0A011NQP2_9PROT        Unreviewed;       427 AA.
AC   A0A011NQP2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:EXI66835.1};
DE            EC=4.4.1.11 {ECO:0000313|EMBL:EXI66835.1};
GN   Name=mdeA_1 {ECO:0000313|EMBL:EXI66835.1};
GN   ORFNames=AW08_02422 {ECO:0000313|EMBL:EXI66835.1};
OS   Candidatus Accumulibacter adjunctus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI66835.1, ECO:0000313|Proteomes:UP000020218};
RN   [1] {ECO:0000313|EMBL:EXI66835.1, 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|ARBA:ARBA00009077, 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:EXI66835.1}.
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DR   EMBL; JFAX01000013; EXI66835.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A011NQP2; -.
DR   STRING; 1454001.AW08_02422; -.
DR   PATRIC; fig|1454001.3.peg.2464; -.
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:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; 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; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR   PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR   PANTHER; PTHR43797:SF2; HOMOCYSTEINE_CYSTEINE SYNTHASE; 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:EXI66835.1};
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   427 AA;  45806 MW;  9B7277EEA3B6E7C5 CRC64;
     MKLETLAVHA GYSPEPTTKA VAVPIYQTTS YSFDSTQHGA DLFDLKVAGN IYTRIMNPTQ
     DVLEKRVAAM EGGIGGLALA SGQAAITYAI MTIAEAGDNI VSASTLYGGT YNLFAHTLPQ
     YGIEVRFANH ADPASFERLI NGRTKALYCE SVGNPLGNIT DFEPLAEIAH RHGVPLIVDN
     TVPSPYLCRP FEHGADIVVH SLTKYIGGHG NSIGGMIVDS GRFPWAEHKL KFRRLNEPDV
     SYHGVVYTEA LGPAAFIGRA RVVPLRNMGA AISPMNSFLI LQGLETLPLR MDRICSNAEK
     VAAYLRAHAK VAWVNYAGLA DHPDHPLVDK YMDGRASGIL TFGVQGSDCS GSVAGARFQD
     ALQLFTRLVN IGDAKSLACH PASTTHRQLG AAELAKAGVS EEMIRLSIGI EHIDDLVADL
     EQALAAV
//
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