ID   C7NKR3_KYTSD            Unreviewed;       468 AA.
AC   C7NKR3;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=O-acetylhomoserine sulfhydrolase {ECO:0000313|EMBL:ACV05549.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:ACV05549.1};
GN   OrderedLocusNames=Ksed_04790 {ECO:0000313|EMBL:ACV05549.1};
OS   Kytococcus sedentarius (strain ATCC 14392 / DSM 20547 / CCM 314 / 541)
OS   (Micrococcus sedentarius).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae;
OC   Kytococcus.
OX   NCBI_TaxID=478801 {ECO:0000313|EMBL:ACV05549.1, ECO:0000313|Proteomes:UP000006666};
RN   [1] {ECO:0000313|EMBL:ACV05549.1, ECO:0000313|Proteomes:UP000006666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14392 / DSM 20547 / CCM 314 / 541
RC   {ECO:0000313|Proteomes:UP000006666};
RX   PubMed=21304632; DOI=10.4056/sigs.761;
RA   Sims D., Brettin T., Detter J.C., Han C., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA   Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA   Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Schneider S.,
RA   Goker M., Pukall R., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Kytococcus sedentarius type strain (541).";
RL   Stand. Genomic Sci. 1:12-20(2009).
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; CP001686; ACV05549.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7NKR3; -.
DR   STRING; 478801.Ksed_04790; -.
DR   KEGG; kse:Ksed_04790; -.
DR   eggNOG; COG2873; Bacteria.
DR   HOGENOM; CLU_018986_4_0_11; -.
DR   Proteomes; UP000006666; 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:ACV05549.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Transferase {ECO:0000313|EMBL:ACV05549.1}.
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         240
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   468 AA;  48873 MW;  D0D16571C8CE57AD CRC64;
     MTHPTEPTPT TDADTTTDTT ADAVSTPSAA PDPSAWGLAT RSIHAGQVPD SDSGSRALPI
     HQTTSYVFAD ADQAANRFAL AELGPIYTRL TNPTTEAVEN RLAALDGGVG ALLLSSGQSA
     TTFSLLNLCR AGDHVVASAH LYGGTQNLLA VTLEKLGIHT TFVDEPNDPA AWREATRGNT
     KAWFAETIAN PSGLVLDIRP VADAAHEAGV PLIVDNTVAT PALLRPLEHG ADVVVYSATK
     FLGGHGTAIA GAIVDGGTFD YGAQPERFPN FTEPDPSYNG LVFARDLGAD GAFGVNLSYV
     LRARVCLLRD LGSAPAPFNA WLIAQGLETL TLRLQKHVAN AHEVASWLDA RPEVTRVQWA
     GLPGHPSHEV AQRYLPDGPG SVLSFELAGG ADAGRAFVSA LKLFSHVANI GDVRSLVIHP
     ASTTHAQLSD AERLAAGVTP GLVRLSVGIE DSADLLADLE RGLAAVAR
//