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Database: UniProt
Entry: A0A075KJ49_9FIRM
LinkDB: A0A075KJ49_9FIRM
Original site: A0A075KJ49_9FIRM 
ID   A0A075KJ49_9FIRM        Unreviewed;       432 AA.
AC   A0A075KJ49;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=O-acetylhomoserine/O-acetylserine sulfhydrylase {ECO:0000313|EMBL:AIF52398.1};
DE            EC=2.5.1.47 {ECO:0000313|EMBL:AIF52398.1};
GN   ORFNames=UFO1_2855 {ECO:0000313|EMBL:AIF52398.1};
OS   Pelosinus sp. UFO1.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=484770 {ECO:0000313|EMBL:AIF52398.1, ECO:0000313|Proteomes:UP000027983};
RN   [1] {ECO:0000313|EMBL:AIF52398.1, ECO:0000313|Proteomes:UP000027983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UFO1 {ECO:0000313|EMBL:AIF52398.1};
RX   PubMed=25189589;
RA   Brown S.D., Utturkar S.M., Magnuson T.S., Ray A.E., Poole F.L.,
RA   Lancaster W.A., Thorgersen M.P., Adams M.W., Elias D.A.;
RT   "Complete Genome Sequence of Pelosinus sp. Strain UFO1 Assembled Using
RT   Single-Molecule Real-Time DNA Sequencing Technology.";
RL   Genome Announc. 2:e00881-14(2014).
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; CP008852; AIF52398.1; -; Genomic_DNA.
DR   RefSeq; WP_038671831.1; NZ_CP008852.1.
DR   AlphaFoldDB; A0A075KJ49; -.
DR   STRING; 484770.UFO1_2855; -.
DR   KEGG; puf:UFO1_2855; -.
DR   eggNOG; COG2873; Bacteria.
DR   HOGENOM; CLU_018986_4_0_9; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000027983; Chromosome.
DR   GO; GO:0004124; F:cysteine synthase 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027983};
KW   Transferase {ECO:0000313|EMBL:AIF52398.1}.
FT   MOD_RES         211
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   432 AA;  47137 MW;  16CA00C1E178D22E CRC64;
     MSEQERKHGF DTVALHAGQI PDRETGARAV PIYQSTSFVL GDTERAARIF ALEEFGNAYT
     RMMNPTQTAF EERVAALEGG VGALAVASGQ AAITYSILNI AQSGDEIVSS SAIYGGTYNL
     FHHTLPKLGI KVHFINPDDP ENFRKAITSK TKALYAEVIG NPRIDVLDIE NVAKVAHENS
     IPLIVDSTFA TPYLNRPIEW GADIVVHSAT KFIGGHGTSI GGIIVDSGNF NWNNGKFPGL
     VEADPSYHGL SFTEKFGNAA YIFRARVTLL RDIGAAITPF NSFLFLQGLE TLSVRLDRHV
     RNTQKVAEFL EQHKFVSWVS YPGLKSNKYY ELGQKYFPKG AGAILTFGIH GGLKAGTKFI
     NNLGLFSHLA NVGDAKSLVI HPASTTHQQL LPAQQLSCGI TEDLVRLSIG LEDIDDLLYY
     LEEALEASHL AD
//
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