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Database: UniProt
Entry: A8TS50_9PROT
LinkDB: A8TS50_9PROT
Original site: A8TS50_9PROT 
ID   A8TS50_9PROT            Unreviewed;       609 AA.
AC   A8TS50;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=O-acetylhomoserine/O-acetylserine sulfhydrylase {ECO:0000313|EMBL:EDP64476.1};
GN   ORFNames=BAL199_27001 {ECO:0000313|EMBL:EDP64476.1};
OS   alpha proteobacterium BAL199.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP64476.1, ECO:0000313|Proteomes:UP000003417};
RN   [1] {ECO:0000313|EMBL:EDP64476.1, ECO:0000313|Proteomes:UP000003417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL199 {ECO:0000313|EMBL:EDP64476.1,
RC   ECO:0000313|Proteomes:UP000003417};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|ARBA:ARBA00009077}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDP64476.1}.
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DR   EMBL; ABHC01000008; EDP64476.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8TS50; -.
DR   STRING; 331869.BAL199_27001; -.
DR   eggNOG; COG2873; Bacteria.
DR   OrthoDB; 9790858at2; -.
DR   Proteomes; UP000003417; Unassembled WGS sequence.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; PF13380; CoA_binding_2; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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   Reference proteome {ECO:0000313|Proteomes:UP000003417}.
FT   DOMAIN          24..120
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   609 AA;  65800 MW;  4C1FB64CC1BA389E CRC64;
     MAEIDPTRAV VHDAYSDDYI RDILRNVKTI AMVGASDNWN RPSYFAMKYL QQKGYRVFPV
     NPKVAAAGGE ILGEKAYADL KDLPETADMV DVFRNSAAAG PVTDAAIEHG TKVVWMQLGV
     RNDEAAERAE KAGIQVVMNR CPKIEFSRLF GELGWHGFNS RVISSKRRTP GSSDAVKGDS
     DVGDGFIAKG FETLAVHAGA APDPTTGARA TPIYQTTAYV FDDVDHAASL FNLQTFGNIY
     SRLSNPTVAV LEERIAALEG GHGTTCTASG HSAQLLALFA LMGPGDRFVA STRLYGGSIT
     QFGRTFKKFD WHCDFVDVED LDATRQAALH PKCKAIFAES LANPGGVITD MQALARIADE
     AGVPLIIDNT MATPYLCRPF EHGADIVVHS TTKFLSGHGN AMGGAVVDGG KFDWSKNDKF
     PSLSQPEPAY HGLTFFETFG DLAYTIYGHA VGLRDLGPTM APMNAYLTIT GIETLALRME
     RHVANAQKIA EWLNAHPKVA WVSYAGLPGN RYHELANRYL PKGAGSVFTF GVVGGYQAGV
     RAVERCRLLS HLANIGDTRS LILHPASTTH RQLTDEQRTT AGAGDDVIRL SIGLESAEDI
     MADLDRALG
//
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