ID   A0A1X7IFC4_9BURK        Unreviewed;       465 AA.
AC   A0A1X7IFC4;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:SMG13056.1};
GN   ORFNames=SAMN06265784_101617 {ECO:0000313|EMBL:SMG13056.1};
OS   Paraburkholderia susongensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1515439 {ECO:0000313|EMBL:SMG13056.1, ECO:0000313|Proteomes:UP000193228};
RN   [1] {ECO:0000313|Proteomes:UP000193228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29540 {ECO:0000313|Proteomes:UP000193228};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) 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; FXAT01000001; SMG13056.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7IFC4; -.
DR   STRING; 1515439.SAMN06265784_101617; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000193228; 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; 2.
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          426..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         207
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   465 AA;  49229 MW;  3C203AE9F6CE6091 CRC64;
     MSANRFDTLA LHAGAAPDPA TGARATPIYQ TTSFSFRDPD HAAALFNMER AGHVYSRISN
     PTVAVFEERV AALENGAGAI GTASGQAALH LAIVTLMGAG SHIVASSALY GGSHNLLHYT
     LRRFGIETTF VKPGDIDAWR AALRPNTRLL FGETLGNPGL DVLDIAAVAQ IAHEHRVPLL
     VDSTFTTPYL LRPFEHGADF VYHSATKFLG GHGTTIGGVL VDGGTFDFDA SGRFPELTEP
     YEGFHGMVFA EESTVAPFLL RARREGLRDF GACLHPQAAW QLLQGIETLP LRMERHVANT
     RRVVEFLAAH AAVETVAYPE LPTHPDHALA QRLLPRGAGA VFSFNLRGDR AAGRAFIEAL
     SLFSHLANVG DARSLVIHPA STTHFRMDAA ALAAAGIAEG TIRLSIGLED PDDLIDDLKR
     ALKAAQKAAQ SGGGTASQQP NTANAASSGT SASSAQLPSS RPESA
//