ID Q0HY40_SHESR Unreviewed; 430 AA.
AC Q0HY40;
DT 03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=O-acetylhomoserine/O-acetylserine sulfhydrylase {ECO:0000313|EMBL:ABI41965.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:ABI41965.1};
GN OrderedLocusNames=Shewmr7_0966 {ECO:0000313|EMBL:ABI41965.1};
OS Shewanella sp. (strain MR-7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60481 {ECO:0000313|EMBL:ABI41965.1};
RN [1] {ECO:0000313|EMBL:ABI41965.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MR-7 {ECO:0000313|EMBL:ABI41965.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of Chromosome1 of Shewanella sp. MR-7.";
RL Submitted (AUG-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}.
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; CP000444; ABI41965.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0HY40; -.
DR KEGG; shm:Shewmr7_0966; -.
DR HOGENOM; CLU_018986_4_2_6; -.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Transferase {ECO:0000313|EMBL:ABI41965.1}.
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 430 AA; 45942 MW; 83DB2DC3C7878E77 CRC64;
MKLESLALHH GYESEATTKA AAVPIYQTTS YTFDDTQHGA DLFDLKVAGN IYTRIMNPTT
SVLEQRLAAI EGGIGALALA SGMAAITYAI QALTQVGDNI VSTSQLYGGT YNLFAHTLPR
QGVEVRMAAF DDFEELDALI DAKTKALFCE SIGNPAGNIV DLKRLAEIAH KHGVPLIVDN
TVATPVLCRP FEHGADIVIH SLTKYIGGHG TTIGGVIIDS GKFDWVANKE RFALLNQADP
SYHGVVYTEA FGAAAFIGRC RVVPLRNTGA ALSPHSAFLL LQGLETLSLR MERHCSNALA
LAEYLILHPS VSWVNYGALP SSPYRENCQK ITGGKASGII SFGIKAATPE EGKIAGGKFI
DALQMILRLV NIGDAKSLAC HPASTTHRQL DANELARAGV SEDLIRISVG IEHIDDIIAD
VAQALEKALA
//
