ID A0A136MQE2_9BACT Unreviewed; 437 AA.
AC A0A136MQE2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Methionine gamma-lyase {ECO:0000313|EMBL:KXK36057.1};
DE EC=4.4.1.11 {ECO:0000313|EMBL:KXK36057.1};
GN Name=mdeA {ECO:0000313|EMBL:KXK36057.1};
GN ORFNames=UZ16_OP3001001607 {ECO:0000313|EMBL:KXK36057.1};
OS Candidatus Hinthialibacteria bacterium OLB16.
OC Bacteria; Candidatus Hinthialibacterota.
OX NCBI_TaxID=1617433 {ECO:0000313|EMBL:KXK36057.1, ECO:0000313|Proteomes:UP000070296};
RN [1] {ECO:0000313|EMBL:KXK36057.1, ECO:0000313|Proteomes:UP000070296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB16 {ECO:0000313|EMBL:KXK36057.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) 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:KXK36057.1}.
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DR EMBL; LMZT01000082; KXK36057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136MQE2; -.
DR STRING; 1617433.UZ16_OP3001001607; -.
DR PATRIC; fig|1617433.3.peg.1736; -.
DR Proteomes; UP000070296; 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:KXK36057.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2}.
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 437 AA; 47559 MW; 81150B126BFE33A0 CRC64;
MSQTEKQGIE TIALHGGQIP DPTTNSRAVP IYQTTSYVFN SAEHAANLFA LKEFGNIYTR
LMNPTTDVLE KRLALLDGGT GALAVASGQA AITLSILNIT QAGQNIVAAS YLYGGTYNLF
HYTFPKLGIK VKFVDSSKPS EVEKAIDDNT RLVYMESIGN PKNNVDDFPA ISDIAHRHGI
PFFIDNTVSP PPIFRPFDWG ADVSVYSLTK FIGGHGTSIG GAIVDSGKFN WNNGKFPELV
EPDPSYHGVS YWQAFGLHDK AVVPGIAYII KVRVQLLRDI GATLSPFNSF LFLQGLETLP
LRVREHARNA QAVAEWLEKH PAVSWVNYPG LPSHSDHERA KKFLKEGCGA IIGFGIKGGR
EAGIKLINSV KLLSHLANIG DAKSLIIHPA STTHQQLSPE EQLSTGVTDD FVRLTVGIES
LEDILADLDQ ALKASQK
//
