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Database: UniProt
Entry: A0A0N1CWX1_9MICO
LinkDB: A0A0N1CWX1_9MICO
Original site: A0A0N1CWX1_9MICO 
ID   A0A0N1CWX1_9MICO        Unreviewed;       430 AA.
AC   A0A0N1CWX1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:KPG80174.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:KPG80174.1};
GN   ORFNames=AEQ27_12315 {ECO:0000313|EMBL:KPG80174.1};
OS   Frigoribacterium sp. RIT-PI-h.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Frigoribacterium.
OX   NCBI_TaxID=1690245 {ECO:0000313|EMBL:KPG80174.1, ECO:0000313|Proteomes:UP000037934};
RN   [1] {ECO:0000313|Proteomes:UP000037934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIT-PI-h {ECO:0000313|Proteomes:UP000037934};
RA   Tran P.N., Lee Y.P., Gan H.M., Savka M.A.;
RT   "Whole genome sequencing of endophytes isolated from poison ivy
RT   (Toxicodendron radicans).";
RL   Submitted (JUL-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:KPG80174.1}.
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DR   EMBL; LHOZ01000082; KPG80174.1; -; Genomic_DNA.
DR   RefSeq; WP_054146910.1; NZ_LHOZ01000082.1.
DR   AlphaFoldDB; A0A0N1CWX1; -.
DR   PATRIC; fig|1690245.3.peg.1606; -.
DR   Proteomes; UP000037934; 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.
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   Reference proteome {ECO:0000313|Proteomes:UP000037934};
KW   Transferase {ECO:0000313|EMBL:KPG80174.1}.
FT   MOD_RES         209
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   430 AA;  45799 MW;  45E45FC4CC3E9477 CRC64;
     MADREYGFRT RAIHAGNIPD AATGARALPI YQTSAFVFDD TDDAAARFAL QKYGNIYSRL
     ANPTTASFEE RVASLEGGLG AVATASGLSA QFVTFASLAG AGDHIVASAN LYGGSLTQLD
     VTLRRFGVET TFVQSSDPAD YAAAIRPETK LLFVETVANP SGEVADLEGL ADVAHAHGLP
     LIVDSTIATP YLNRPIEWGA DVVVHSATKF LGGHGTTLGG VVVESGRFDW DSERFPLFDQ
     PVPSYGGLNW SGNFGEYAFL TRLRAEQLRD IGPALAPHSA FLLAQGVETL PFRMQAHVDN
     ARQVAEWLDA DPRIERVRWA GLPGHPHHDR AAKYLPKGPG SVFTFELKGG RPAGKTFIES
     VELASHLANI GDAKTLVIHP GSTTHAQLSE QQLVDAGVLP GSVRISVGIE DPDDIIHDLD
     QALAAATKGE
//
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