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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//