ID K4L582_9FIRM Unreviewed; 426 AA.
AC K4L582;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=O-acetylhomoserine sulfhydrylase / O-succinylhomoserine sulfhydrylase {ECO:0000313|EMBL:AFV05751.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:AFV05751.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:AFV05751.1};
GN ORFNames=DCF50_p1749 {ECO:0000313|EMBL:AFV05751.1};
OS Dehalobacter sp. CF.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Dehalobacter.
OX NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV05751.1, ECO:0000313|Proteomes:UP000000482};
RN [1] {ECO:0000313|EMBL:AFV05751.1, ECO:0000313|Proteomes:UP000000482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF {ECO:0000313|EMBL:AFV05751.1};
RX PubMed=23284863; DOI=10.1371/journal.pone.0052038;
RA Tang S., Gong Y., Edwards E.A.;
RT "Semi-automatic in silico gap closure enabled de novo assembly of two
RT dehalobacter genomes from metagenomic data.";
RL PLoS ONE 7:E52038-E52038(2012).
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}.
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DR EMBL; CP003870; AFV05751.1; -; Genomic_DNA.
DR RefSeq; WP_015043797.1; NC_018867.1.
DR AlphaFoldDB; K4L582; -.
DR STRING; 1131462.DCF50_p1749; -.
DR KEGG; dec:DCF50_p1749; -.
DR PATRIC; fig|1131462.4.peg.1763; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_9; -.
DR Proteomes; UP000000482; Chromosome.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
DR GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IEA:UniProtKB-EC.
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; 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:UP000000482};
KW Transferase {ECO:0000313|EMBL:AFV05751.1}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 426 AA; 45684 MW; 69B32294B26D7E27 CRC64;
MSKENWKFDT LQVHAGQVPD PTTGSRAVPI YQTTSYVFRD AKHGADLFSL AEPGNIYTRI
MNPTSDVLEQ RIAALEGGVG ALAVGSGSAA ITYAILNIAG AGDEIISAST LYGGTHNLFA
ITLPKLGIKT HFVNPDDPAN FKKAITEKTK AIYIESIGNP GINIIDIEAV AKVAHDNGIP
LIIDNTFATP YLLRPIEYGA DIVVHSATKF IGGHGTSIGG LIIDGGKFDW AASGKFPGFT
EPDPSYNGLV YATLGAPAFI LKARVQLLRD TGAALSPFNS FLFIQGLETL SLRVKQHVAN
TWKVVDYLKN HLKVSWVNYP GLKDNKYFDL SLKYFPQGPG SIFTFGIKGG AEAGVKLINN
LELFSLLANV ADAKSLVIHP ASTTHAQLSE EEQRAAGVTP DMIRLSIGIE DADDIIADLE
QAFAKL
//
