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Database: UniProt
Entry: W8F2X9_9BACT
LinkDB: W8F2X9_9BACT
Original site: W8F2X9_9BACT 
ID   W8F2X9_9BACT            Unreviewed;       460 AA.
AC   W8F2X9;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:AHJ99303.1};
GN   ORFNames=Hsw_3708 {ECO:0000313|EMBL:AHJ99303.1};
OS   Hymenobacter swuensis DY53.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1227739 {ECO:0000313|EMBL:AHJ99303.1, ECO:0000313|Proteomes:UP000019423};
RN   [1] {ECO:0000313|EMBL:AHJ99303.1, ECO:0000313|Proteomes:UP000019423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY53 {ECO:0000313|EMBL:AHJ99303.1,
RC   ECO:0000313|Proteomes:UP000019423};
RA   Jung J.-H., Jeong S.-W., Joe M.-H., Cho y.-j., Kim M.-K., Lim S.-Y.;
RT   "Complete genome sequence of ionizing-radiation resistance bacterium
RT   Hymenobacter swuensis DY53.";
RL   Submitted (JAN-2014) 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; CP007145; AHJ99303.1; -; Genomic_DNA.
DR   RefSeq; WP_044003356.1; NZ_CP007145.1.
DR   AlphaFoldDB; W8F2X9; -.
DR   STRING; 1227739.Hsw_3708; -.
DR   KEGG; hsw:Hsw_3708; -.
DR   PATRIC; fig|1227739.3.peg.3864; -.
DR   eggNOG; COG2873; Bacteria.
DR   HOGENOM; CLU_018986_4_0_10; -.
DR   OrthoDB; 634606at2; -.
DR   Proteomes; UP000019423; Chromosome.
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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019423}.
FT   REGION          440..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   460 AA;  49952 MW;  A56979A727CFA195 CRC64;
     MSTQNFHFET LQLHAGQQPD PITGSRAVPI HQTTSYVFKN AEHGANLFAL KEFGNIYTRL
     MNPTTDVFEQ RVAALEGGVA ALAVSSGQAA QFIALNNILQ AGDNFVSTTH LYGGTYNQFK
     VAFKRLGIEV RFADGDQPSK FEALIDEKTK AIYLETIGNP SFSIPDFEAI AAIANKHDLP
     LIVDNTFGAG GYLFRPLEHG ASIVVESATK WIGGHGTSVG GVIVDGGTYD FGNGKFPQFT
     EPSDGYHGLI FNDVFGKNGP FGNIAFIIRA RVEGLRDFGP SQSPFNSFLL LQGLETLSLR
     VERTVENALR VATWLEQHPQ VEAVNYPGLP SSPYHKLAQK YLKRGYGGVL TFAIKGSKET
     ATQFIDNLKL VSHLANVGDA KTLIIQPSAT THQQLSDEEQ RAAGVLPTLL RLSVGIEHFD
     DIRADLQQAF DAVRNAATPN TAEGTLLPEP ETEHAAPLEV
//
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