ID   Q2GA65_NOVAD            Unreviewed;       427 AA.
AC   Q2GA65;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=O-acetylhomoserine sulfhydrolase {ECO:0000313|EMBL:ABD25258.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:ABD25258.1};
GN   OrderedLocusNames=Saro_0813 {ECO:0000313|EMBL:ABD25258.1};
OS   Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS   56034 / CIP 105152 / NBRC 16084 / F199).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238 {ECO:0000313|EMBL:ABD25258.1, ECO:0000313|Proteomes:UP000009134};
RN   [1] {ECO:0000313|Proteomes:UP000009134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC   / F199 {ECO:0000313|Proteomes:UP000009134};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA   Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT   "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL   Submitted (JAN-2006) 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; CP000248; ABD25258.1; -; Genomic_DNA.
DR   RefSeq; WP_011444472.1; NC_007794.1.
DR   AlphaFoldDB; Q2GA65; -.
DR   STRING; 279238.Saro_0813; -.
DR   KEGG; nar:Saro_0813; -.
DR   eggNOG; COG2873; Bacteria.
DR   HOGENOM; CLU_018986_4_0_5; -.
DR   Proteomes; UP000009134; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ABD25258.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009134};
KW   Transferase {ECO:0000313|EMBL:ABD25258.1}.
FT   MOD_RES         206
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   427 AA;  44859 MW;  7C03AFDB504A24AE CRC64;
     MTQKLETLTV HAGCEPDPTT KARITPIYQT ASYVFDSAEH AANLFALAEF GNIYSRIMNP
     TNAALEAKIA ALEGGVAALG VASGHAAQFI VFHTLMEPGC EIVAAKKLYG GTLNQFAHGF
     AKFGWKAVFV DADDPAAVAA AITDKTRGVF IESLANPGGV VQDIAAIAEV AHAAGVPLIV
     DNTMASPALC RPIEHGADIV VHSCTKFLNG HGNSIGGLIV DAGRFDWAAS DKFPSLSQPN
     PSYHGAVLTE ALKPVGPIAF IIGCRVLGLR DLGPAMAPMN AFLTLTGMET LALRIERHCA
     NALHLAQWLQ NHPKVAWVSY AGLPEDPYHQ LAKQYLGGKG GAVFTFGVKG GYEAGVKLVQ
     SVKLFSHLAN IGDTRSLIIH PASTTHSQLG EEELVAAGAG PDTVRVSVGI EHIDDIVADL
     AQALELV
//