ID D4MNT3_9FIRM Unreviewed; 431 AA.
AC D4MNT3;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=O-acetylhomoserine sulfhydrolase {ECO:0000313|EMBL:CBL35416.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:CBL35416.1};
GN ORFNames=ES1_26260 {ECO:0000313|EMBL:CBL35416.1};
OS [Eubacterium] siraeum V10Sc8a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=717961 {ECO:0000313|EMBL:CBL35416.1, ECO:0000313|Proteomes:UP000007050};
RN [1] {ECO:0000313|EMBL:CBL35416.1, ECO:0000313|Proteomes:UP000007050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V10Sc8a {ECO:0000313|EMBL:CBL35416.1,
RC ECO:0000313|Proteomes:UP000007050};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Eubacterium siraeum V10Sc8a.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL35416.1, ECO:0000313|Proteomes:UP000007050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V10Sc8a {ECO:0000313|EMBL:CBL35416.1,
RC ECO:0000313|Proteomes:UP000007050};
RA Pajon A.;
RL Submitted (MAR-2010) 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}.
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DR EMBL; FP929059; CBL35416.1; -; Genomic_DNA.
DR AlphaFoldDB; D4MNT3; -.
DR KEGG; esr:ES1_26260; -.
DR PATRIC; fig|717961.3.peg.228; -.
DR HOGENOM; CLU_018986_4_0_9; -.
DR BioCyc; ESIR717961:G136L-2212-MONOMER; -.
DR Proteomes; UP000007050; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:CBL35416.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Transferase {ECO:0000313|EMBL:CBL35416.1}.
FT MOD_RES 213
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 431 AA; 46510 MW; 3FCBB0DAB8D352D9 CRC64;
MSYTYDNNYR FETIQLHAGQ ETPDPASDAR AVPIYQTTSY VFKNSAHAAA RFGLADAGNI
YGRLTNSTQG AFETRIAALE GGVAALATAS GAAAITYAIQ ALAYAGEHIV AQKTIYGGSY
NLLAHTLPQY GISTTFVDAH NLEEVENAIQ DNTKAIYLET LGNPNSDIPD IDAIAEIAHK
HGLPLVIDNT FGTPYLIRPI EHGADVVVHS ATKFIGGHGT TLGGVIVDSG KFDWKKSGKY
APIAEPNPSY HGVSFVDAAG PAAFVTYIRA ILLRDTGATI SPFNAFLLLQ GTETLSLRLD
RHIENTKKVV EFLANHPKVE KVNHPSLPDH PDHALYTKYF KNGGASIFTF NIKGGQEEAH
KFIDSLQIFS LLANVADVKS LVIHPATTTH SQLTDEELAD QGIGRNTIRL SIGTEHIDDI
IADLSQAFDK V
//
