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Database: UniProt
Entry: J9YY50_9PROT
LinkDB: J9YY50_9PROT
Original site: J9YY50_9PROT 
ID   J9YY50_9PROT            Unreviewed;       442 AA.
AC   J9YY50;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:AFS48634.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:AFS48634.1};
GN   ORFNames=HIMB59_00004340 {ECO:0000313|EMBL:AFS48634.1};
OS   alpha proteobacterium HIMB59.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC   Candidatus Pelagibacteraceae.
OX   NCBI_TaxID=744985 {ECO:0000313|EMBL:AFS48634.1, ECO:0000313|Proteomes:UP000006097};
RN   [1] {ECO:0000313|EMBL:AFS48634.1, ECO:0000313|Proteomes:UP000006097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HIMB59 {ECO:0000313|EMBL:AFS48634.1,
RC   ECO:0000313|Proteomes:UP000006097};
RA   Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., Giovannoni S.J.,
RA   Rappe M.S., Brinkac L., Kim M., Beeson K., Ferriera S., Sutton G.,
RA   Friedman R., Venter J.C.;
RL   Submitted (AUG-2012) 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; CP003801; AFS48634.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9YY50; -.
DR   STRING; 744985.HIMB59_00004340; -.
DR   KEGG; apc:HIMB59_00004340; -.
DR   PATRIC; fig|744985.3.peg.432; -.
DR   eggNOG; COG2873; Bacteria.
DR   HOGENOM; CLU_018986_4_2_5; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000006097; 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   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:UP000006097};
KW   Transferase {ECO:0000313|EMBL:AFS48634.1}.
FT   MOD_RES         209
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   442 AA;  47398 MW;  07E1B125C114A03D CRC64;
     MTTTSKHPET LALHGGSYRK DPTTNAVAVP IYQTTSYEFN STEHAGNLFA LKELGNIYTR
     IMNPTNAVLE ERLAAIEGGA AALALSSGQA ASAFSIQNVA QAGDNIVCST DIYGGTWNLF
     NNTLRAQGID VRFADPSDPE NFRKLTDDKT RAYYAETLPN PKLSVFPIEE VANIGRPLGI
     PLIVDNTAAP LSCKPFDYGA AIVMHSLTKW IGGHGTSIGG IIIDGGNFDW TAVPERQPFY
     NQPDSSYHGA VWGDVVPQIF GVQIAFAIRA RVVLLRDLGA AIAPQNSFNL IQGLESLPLR
     IKQHNANALE VADFLKGHDQ VSKVTFPKFA EGKAKENADK YLNGNYGSMI GIEVKNGVEG
     GKAFIDALQL HYHVANIGDS RSLAIHPAST THSQLSAEEQ LKAGVTPGYV RLCVGIEHVE
     DIIEDLKIGL EAASKATATA AA
//
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