ID   METY_LEPME              Reviewed;         442 AA.
AC   P94890;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=O-acetyl-L-homoserine sulfhydrylase {ECO:0000303|PubMed:9440513};
DE            Short=OAH-sulfhydrylase {ECO:0000303|PubMed:12832650};
DE            EC=2.5.1.- {ECO:0000269|PubMed:12832650, ECO:0000269|PubMed:9440513};
GN   Name=metY {ECO:0000303|PubMed:9209059};
OS   Leptospira meyeri.
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=29508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serovar Semaranga / isolate Veldrat S 173;
RX   PubMed=9209059; DOI=10.1128/jb.179.13.4396-4398.1997;
RA   Bourhy P., Martel A., Margarita D., Saint Girons I., Belfaiza J.;
RT   "Homoserine O-acetyltransferase, involved in the Leptospira meyeri
RT   methionine biosynthetic pathway, is not feedback inhibited.";
RL   J. Bacteriol. 179:4396-4398(1997).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PATHWAY.
RC   STRAIN=Serovar Semaranga / isolate Veldrat S 173;
RX   PubMed=9440513; DOI=10.1128/jb.180.2.250-255.1998;
RA   Belfaiza J., Martel A., Margarita D., Saint Girons I.;
RT   "Direct sulfhydrylation for methionine biosynthesis in Leptospira meyeri.";
RL   J. Bacteriol. 180:250-255(1998).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=12832650; DOI=10.1093/molbev/msg169;
RA   Hacham Y., Gophna U., Amir R.;
RT   "In vivo analysis of various substrates utilized by cystathionine gamma-
RT   synthase and O-acetylhomoserine sulfhydrylase in methionine biosynthesis.";
RL   Mol. Biol. Evol. 20:1513-1520(2003).
CC   -!- FUNCTION: Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into
CC       homocysteine in the methionine biosynthesis pathway (PubMed:9440513,
CC       PubMed:12832650). Can also use O-succinyl-homoserine (OSH), although at
CC       low efficiency (PubMed:12832650). {ECO:0000269|PubMed:12832650,
CC       ECO:0000269|PubMed:9440513}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen sulfide + O-acetyl-L-homoserine = acetate + L-
CC         homocysteine; Xref=Rhea:RHEA:27822, ChEBI:CHEBI:29919,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:57716, ChEBI:CHEBI:58199;
CC         Evidence={ECO:0000269|PubMed:12832650, ECO:0000269|PubMed:9440513};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q5SK88};
CC   -!- ACTIVITY REGULATION: Feedback inhibited at very high concentrations of
CC       methionine or S-adenosylmethionine. {ECO:0000269|PubMed:9440513}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homocysteine from O-acetyl-L-homoserine: step 1/1.
CC       {ECO:0000305|PubMed:9440513}.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000305}.
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DR   EMBL; Y10744; CAA71732.1; -; Genomic_DNA.
DR   PIR; T44655; T44655.
DR   AlphaFoldDB; P94890; -.
DR   SMR; P94890; -.
DR   STRING; 1193051.LEP1GSC017_3349; -.
DR   BioCyc; MetaCyc:MON-9366; -.
DR   BRENDA; 2.5.1.49; 2987.
DR   UniPathway; UPA00051; UER00079.
DR   GO; GO:0051009; F:O-acetylhomoserine sulfhydrylase activity; IEA:RHEA.
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:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR   CDD; cd00614; CGS_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01326; OAH_OAS_sulfhy; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Methionine biosynthesis; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN           1..442
FT                   /note="O-acetyl-L-homoserine sulfhydrylase"
FT                   /id="PRO_0000445419"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         216
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SK88"
SQ   SEQUENCE   442 AA;  47961 MW;  75685C484E11F80A CRC64;
     MVGPSGESMP RNFKPETIAL HGGQEPDPTT TSRAVPLYQT TSYVFKDTDH AARLFGLQEF
     GNIYTRLMNP TTDVLEKRVA ALEGGVAALA TASGQSAEML ALLNIVEAGQ EIVASSSLYG
     GTYNLLHYTF PKLGIKVHFV DQSDPENFRK ASNDKTRAFY AETLGNPKLD TLDIAAVSKV
     AKEVGVPLVI DNTMPSPYLV NPLKHGADIV VHSLTKFLGG HGTSIGGIII DGGSFNWGNG
     KFKNFTEPDP SYHGLKFWEV FGKFEPFGGV NIAFILKARV QGLRDLGPAI SPFNAWQILQ
     GVETLPLRME RHSGNALKVA EFLQKHPKIE WVNYPGLSTD KNYATAKKYH ERGLFGAIVG
     FEIKGGVEKA KKFIDGLELF SLLANIGDAK SLAIHPASTT HQQLTGPEQI SAGVTPGFVR
     LSVGLENIDD ILVDLEEALK NI