ID   A0A3A5MBJ0_9MICO        Unreviewed;       448 AA.
AC   A0A3A5MBJ0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Bifunctional o-acetylhomoserine/o-acetylserine sulfhydrylase {ECO:0000313|EMBL:RJT87477.1};
GN   ORFNames=D6T64_14275 {ECO:0000313|EMBL:RJT87477.1};
OS   Cryobacterium melibiosiphilum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=995039 {ECO:0000313|EMBL:RJT87477.1, ECO:0000313|Proteomes:UP000272015};
RN   [1] {ECO:0000313|EMBL:RJT87477.1, ECO:0000313|Proteomes:UP000272015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hh39 {ECO:0000313|EMBL:RJT87477.1,
RC   ECO:0000313|Proteomes:UP000272015};
RA   Liu Q., Xin Y.-H.;
RT   "Novel species of Cryobacterium.";
RL   Submitted (SEP-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RJT87477.1}.
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DR   EMBL; QZVS01000089; RJT87477.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A5MBJ0; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000272015; Unassembled WGS sequence.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         211
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   448 AA;  47635 MW;  4E234BDB29008EDE CRC64;
     MSDTSAWKFE TKQVHSGARP DPVTNARATP IYQTTSYVFN SAEHAQNLFA LAEFGNIYTR
     IQNPTQAVVE ERVAALEGGT GALLLASGQS ASNFAVLNIA QAGDHIVSSS SIYGGTYNLF
     KYSLAKLGIE TTFVENQDDA EEWRRAVRPN TKLFFAETIG NPQINVLDIR LVADVAHAAG
     VPLIVDNTIA TPYLIRPFEH GADIIVHSAT KFLGGHGTII GGVLVDGGTF EWSKNVEKFP
     GLTEPDPSYH GASYTTVLGD GLAYIIKARV QLLRDFGSAI APASAWQLIQ GIETLSLRIE
     RHVQNAQLIA EWLEAHPDIA SVNYAGLPSS PWYAAANRYA PLGVGAVLSF ELTGGVDAGR
     ALVDNLTLFS HLANIGDVRS LVIHPASTTH AQLTPEQQLT AGVTPGLVRL SVGIENIADL
     IADLEAGLSA AAAVTTASRA AARSDITD
//