ID A9BFW2_PETMO Unreviewed; 429 AA.
AC A9BFW2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=O-acetylhomoserine/O-acetylserine sulfhydrylase {ECO:0000313|EMBL:ABX31458.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:ABX31458.1};
GN OrderedLocusNames=Pmob_0734 {ECO:0000313|EMBL:ABX31458.1};
OS Petrotoga mobilis (strain DSM 10674 / SJ95).
OC Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC Petrotoga.
OX NCBI_TaxID=403833 {ECO:0000313|EMBL:ABX31458.1, ECO:0000313|Proteomes:UP000000789};
RN [1] {ECO:0000313|EMBL:ABX31458.1, ECO:0000313|Proteomes:UP000000789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10674 / SJ95 {ECO:0000313|Proteomes:UP000000789};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Noll K., Richardson P.;
RT "Complete sequence of Petroga mobilis SJ95.";
RL Submitted (NOV-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 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; CP000879; ABX31458.1; -; Genomic_DNA.
DR RefSeq; WP_012208561.1; NC_010003.1.
DR AlphaFoldDB; A9BFW2; -.
DR STRING; 403833.Pmob_0734; -.
DR KEGG; pmo:Pmob_0734; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_0; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000000789; 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.
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:ABX31458.1}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 429 AA; 47202 MW; F0E7E1FF44986770 CRC64;
MEERNHNFDT LMVHAGYEKD PTTGANVVPI YQTSSYTFED SAHALRLFNM EETGNIYTRI
MNPTTDVLEK RVAALEGGVG SLATSSGQAA EAIAVLNIME EGDEILTASS LYGGTFTLFK
NSLSRFGIKT HFFDIDDVDS LKNKINNRTK AVYVETIGNP ELSVPDFEQI SKIAHENGIP
LIVDNTFATP YLCRPFEFGA DIVVHSLTKY LNGHGNSIGG IIVDSGNFDW NNGKFNMLTE
EDPAFHGISF YKKFGNAAYI SKARSQWLRD LGASISPFNS FLILQGIETL SLRMERHSSN
AMKIAEFLSE DSRVSWVNYP GLKNHKAHKN AVKYLKHGYG GMLSFGVKGG VEAGKRFIES
LRIFSHVANV GDVRSLAVHP ASTTHGQLSE EEQLASGVSP DMIRLSVGIE DINDLIEDID
SALTKATKN
//
