ID A0A0A2ETH1_PORCN Unreviewed; 425 AA.
AC A0A0A2ETH1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:KGN80972.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:KGN80972.1};
GN ORFNames=HQ35_04915 {ECO:0000313|EMBL:KGN80972.1};
OS Porphyromonas cangingivalis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=36874 {ECO:0000313|EMBL:KGN80972.1, ECO:0000313|Proteomes:UP000030125};
RN [1] {ECO:0000313|EMBL:KGN80972.1, ECO:0000313|Proteomes:UP000030125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-109 OH1386 {ECO:0000313|Proteomes:UP000030125};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas cangingivalis strain:COT-109_OH1386 Genome sequencing.";
RL Submitted (AUG-2014) 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 -!- 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:KGN80972.1}.
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; JQJD01000033; KGN80972.1; -; Genomic_DNA.
DR RefSeq; WP_036851497.1; NZ_JQJD01000033.1.
DR AlphaFoldDB; A0A0A2ETH1; -.
DR STRING; 36874.HQ34_03810; -.
DR eggNOG; COG2873; Bacteria.
DR OrthoDB; 9803729at2; -.
DR Proteomes; UP000030125; Unassembled WGS sequence.
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:UP000030125};
KW Transferase {ECO:0000313|EMBL:KGN80972.1}.
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 425 AA; 46097 MW; 52B8AB8B3C6EC211 CRC64;
MITKTATQAL HAAYDPSSNN GSTAIPLYQA TAYTFESNDH AAGVFDLQKP GYIYTRLNNP
TTDILEQRIA TLDGGIGCIA TASGMSAIST TLLTLLKSGD HIVASSSIYG GTYNLLSVTL
PRLGIKTTFV DPEQPKSFEE AIKPHTKLIY TESLGNPKLD FVDIKEVSRI AHSHGLPLVV
DNTLTPLLFK PIEHGADIVI YSLTKFFCGN GTAMGGAVVD AGKFDWSNGN FPDFTEPSPG
YHGLIYSDVF KEAAFIVRAR VEGLRDFGSC ISPTNSFIIL QGLETLSLRL KQACSNALEI
AQWLKEHPLV EWVHYPGLSS DKHHEVCSRY LNGGFGSLIT FGPKGGYNAA KSVVDSTNIF
RIVANLGDTK SLIIHPSSTT HRQLKEDQQL SAGVTPDLIR LSIGLEDIED LKADLHNALT
QSIQK
//
