ID F5SWL0_9GAMM Unreviewed; 368 AA.
AC F5SWL0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:EGL55476.1};
GN ORFNames=MAMP_02470 {ECO:0000313|EMBL:EGL55476.1};
OS Methylophaga aminisulfidivorans MP.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL55476.1, ECO:0000313|Proteomes:UP000003544};
RN [1] {ECO:0000313|EMBL:EGL55476.1, ECO:0000313|Proteomes:UP000003544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544};
RX PubMed=21685284; DOI=10.1128/JB.05403-11;
RA Han G.H., Kim W., Chun J., Kim S.W.;
RT "Draft genome sequence of Methylophaga aminisulfidivorans MP T.";
RL J. Bacteriol. 193:4265-4265(2011).
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:EGL55476.1}.
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DR EMBL; AFIG01000001; EGL55476.1; -; Genomic_DNA.
DR AlphaFoldDB; F5SWL0; -.
DR STRING; 1026882.MAMP_02470; -.
DR eggNOG; COG2873; Bacteria.
DR Proteomes; UP000003544; Unassembled WGS sequence.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000003544}.
FT MOD_RES 149
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 368 AA; 39823 MW; 690A38DE3250CADF CRC64;
MNPTNDVLEK RLAEMEGGIA GLAVASGMSA ITYAIQAIAE AGDNIVSSTQ LYGGSYNLFA
HTCPRQGITV RMASFDDYDK IESLIDDKTK ALFCESIGNP AGNIVDIQRW AEIAHRHGVP
LIVDNTVATP YLCRVFDHGA DIVVHSLTKY IGGHGTTVGG MIVDSGRFDW VANKERFPML
NEPDPSYHGV IYTEALGPAA YIGRCRVIPL RNTGSALSPH SAFLLMQGLE TLGLRMERHC
ENALKVANYL QQHPKVEWVN YAALENSPYH EVCQKITKGQ ASGILSFGIT GGKEAGARFI
DALQMILRLV NIGDAKSLAC HPATTTHRQL SPEELATAGV SEDLVRISVG IEHIDDIIAD
IAQALEKA
//