ID G4Q7Q8_ACIIR Unreviewed; 431 AA.
AC G4Q7Q8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=O-acetylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:AEQ23578.1};
GN Name=metY {ECO:0000313|EMBL:AEQ23578.1};
GN OrderedLocusNames=Acin_2386 {ECO:0000313|EMBL:AEQ23578.1};
OS Acidaminococcus intestini (strain RyC-MR95).
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Acidaminococcus.
OX NCBI_TaxID=568816 {ECO:0000313|EMBL:AEQ23578.1, ECO:0000313|Proteomes:UP000007093};
RN [1] {ECO:0000313|EMBL:AEQ23578.1, ECO:0000313|Proteomes:UP000007093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RyC-MR95 {ECO:0000313|EMBL:AEQ23578.1,
RC ECO:0000313|Proteomes:UP000007093};
RX PubMed=22123762; DOI=10.1128/JB.06301-11;
RA D'Auria G., Galan J.C., Rodriguez-Alcayna M., Moya A., Baquero F.,
RA Latorre A.;
RT "Complete genome sequence of Acidaminococcus intestini RYC-MR95, a Gram-
RT negative bacterium from the phylum Firmicutes.";
RL J. Bacteriol. 193:7008-7009(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}.
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DR EMBL; CP003058; AEQ23578.1; -; Genomic_DNA.
DR RefSeq; WP_014129165.1; NC_016077.1.
DR AlphaFoldDB; G4Q7Q8; -.
DR STRING; 568816.Acin_2386; -.
DR KEGG; ain:Acin_2386; -.
DR PATRIC; fig|568816.4.peg.2316; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_9; -.
DR InParanoid; G4Q7Q8; -.
DR Proteomes; UP000007093; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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:AEQ23578.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000007093}.
FT MOD_RES 212
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 431 AA; 46491 MW; 670736CE9F031EF7 CRC64;
MSEGKAYHFE TLQLHVGQEQ PDPSTGARAV PIYMSTSYVF KDSAQASDRF ALKDAGFIYS
RLGDPTSDVL EKRLAALEGG VGALVTATGA AAISYTIQAL CHKDDHIVAA TTIYGGTYNL
FAHTLPDFGI ETTFVDPTKG SSVFEGAIRE NTQLLYIETV GNPNANLIDI GAVAEIAHKH
GIPLVVDNTF ATPYLVRPFE FGADIVVHSA TKFIGGHGTT LGGVIVDSGK FDWAASGKFP
WLVEANPSYH GPSFTRDVGA AAFVTYVRAV ILRDLGATLS PFAAFMLLQG TETLSLRVER
QVENALKVVD FLAHDPHVAK VNHPSLDNHP DHELYRRYFP HGGISIFTFE IKGGPEAART
FIDHLKVFSL LANVADVKSL VIHPASTTHS QMTEEELLSS GITPSTIRLS IGAEHIDDIL
EDLKTGFAAL D
//
