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Database: UniProt
Entry: W8S8C1_9RHOB
LinkDB: W8S8C1_9RHOB
Original site: W8S8C1_9RHOB 
ID   W8S8C1_9RHOB            Unreviewed;       397 AA.
AC   W8S8C1;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:AHM05211.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:AHM05211.1};
GN   ORFNames=roselon_02924 {ECO:0000313|EMBL:AHM05211.1};
OS   Roseibacterium elongatum DSM 19469.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseibacterium.
OX   NCBI_TaxID=1294273 {ECO:0000313|EMBL:AHM05211.1, ECO:0000313|Proteomes:UP000019593};
RN   [1] {ECO:0000313|EMBL:AHM05211.1, ECO:0000313|Proteomes:UP000019593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19469 {ECO:0000313|Proteomes:UP000019593};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (MAR-2013) 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|RuleBase:RU362118}.
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DR   EMBL; CP004372; AHM05211.1; -; Genomic_DNA.
DR   RefSeq; WP_025312898.1; NZ_CP004372.1.
DR   AlphaFoldDB; W8S8C1; -.
DR   STRING; 1294273.roselon_02924; -.
DR   KEGG; red:roselon_02924; -.
DR   PATRIC; fig|1294273.3.peg.2886; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_0_5; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000019593; Chromosome.
DR   GO; GO:0003961; F:O-acetylhomoserine aminocarboxypropyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019346; P:transsulfuration; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11808:SF90; CYSTATHIONINE GAMMA-LYASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 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:UP000019593};
KW   Transferase {ECO:0000313|EMBL:AHM05211.1}.
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   397 AA;  42277 MW;  37EB1FC8F7132CDF CRC64;
     MSDDRRNVRP ETLVRRMPLA EGVSRPVVTP IQPSVVYASP SIDTLHAQYE GRETGYTYAR
     EGHPNATVLA RKIDAMEGAE GGLVTGSGMA AVTAALMGIM GAGDHVIGGN QLYGRSLRLM
     HQDLARFGIA TSVADPTDAE AVRAAIRPET RMILLEVVSN PTLRVADMEG IAAVAREAGV
     LLAVDNTFTT PRAWRPFEHG ADIVIHSVTK LLAGHSDVTL GYVVAKDAGL QRAIYDFAVT
     TGLTPSPYEC WLAERGLYTF PLRYDRAEAN AAALADVLAG HPKVKRVLYP GRDDHPDRAR
     AKALLGARTG NMVSFEIDGN EAAANRMVAA APQLPFAPTL GDVGTTLSHP ASSSHRALTP
     DARADLGHES TGSFRVSVGI EEIDLLISDF EQGLAAV
//
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