ID A0A0D6TFG9_9RHOB Unreviewed; 428 AA.
AC A0A0D6TFG9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:KIX18974.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:KIX18974.1};
GN ORFNames=SY26_02250 {ECO:0000313|EMBL:KIX18974.1};
OS Paracoccus sp. 228.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1192054 {ECO:0000313|EMBL:KIX18974.1, ECO:0000313|Proteomes:UP000032743};
RN [1] {ECO:0000313|EMBL:KIX18974.1, ECO:0000313|Proteomes:UP000032743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=361 {ECO:0000313|EMBL:KIX18974.1,
RC ECO:0000313|Proteomes:UP000032743};
RA Karczewska-Golec J., Kochanowska-Lyzen M., Balut M., Golec P.,
RA Madanecki P., Markert S., Piotrowski A., Schweder T., Szalewska-Palasz A.;
RT "Three Bacterial Inhabitants of the Baltic Sea under Osmotic Stress: a
RT Genomic and a Proteomic Perspective.";
RL Submitted (FEB-2015) 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:KIX18974.1}.
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DR EMBL; JYGY01000001; KIX18974.1; -; Genomic_DNA.
DR RefSeq; WP_045999092.1; NZ_JYGY01000001.1.
DR AlphaFoldDB; A0A0D6TFG9; -.
DR STRING; 1192054.SY26_02250; -.
DR PATRIC; fig|1603292.4.peg.456; -.
DR Proteomes; UP000032743; 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:UP000032743};
KW Transferase {ECO:0000313|EMBL:KIX18974.1}.
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 428 AA; 45303 MW; 595CB9290D79765F CRC64;
MSDQQGFDTR AIHAGAAADP ATGARQVPIY QTTAYAFRDA DHAARLFNLQ EVGYIYSRLT
NPTVAALQAR VAALEGGAGA VCCSSGHAAQ IMALFPLMAP GRNIVASTRL YGGTVTQFSH
TIRRFGWSAK FVDFDDPEAL RAAIDDDTRA VFCESISNPG GSVTDIPAVA AIADAAGIPL
IVDNTLATPY LCRPIEMGAT LVVHSLTKYM TGNGTVTGGV VVDSGTFDWS ASDKFPSLSA
PEPAYHGLKF HETFGNMAFT FHGIAIGLRD LGMTMNPQGA HYTLMGIETL GLRMERHVAN
AQKVAAWLEA DDRVERVTYA GLDSSPWNTT ARRLYPKGAG ALFTFAIRGG YAAAVKLVDA
LSLFSHVANL GDARSLVIHS ASTTHRQLTE DQQRAAGAAP EVVRLSVGIE DAGDLIADLD
QALAKATA
//
