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Database: UniProt
Entry: A0A0R2RQ35_9PROT
LinkDB: A0A0R2RQ35_9PROT
Original site: A0A0R2RQ35_9PROT 
ID   A0A0R2RQ35_9PROT        Unreviewed;       442 AA.
AC   A0A0R2RQ35;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:KRO64502.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:KRO64502.1};
GN   ORFNames=ABS03_02155 {ECO:0000313|EMBL:KRO64502.1};
OS   Pelagibacteraceae bacterium BACL5 MAG-120820-bin39.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC   Candidatus Pelagibacteraceae.
OX   NCBI_TaxID=1655605 {ECO:0000313|EMBL:KRO64502.1, ECO:0000313|Proteomes:UP000051468};
RN   [1] {ECO:0000313|EMBL:KRO64502.1, ECO:0000313|Proteomes:UP000051468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL5 MAG-120820-bin39 {ECO:0000313|EMBL:KRO64502.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA   Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-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:KRO64502.1}.
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DR   EMBL; LIBV01000046; KRO64502.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2RQ35; -.
DR   Proteomes; UP000051468; 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   Transferase {ECO:0000313|EMBL:KRO64502.1}.
FT   MOD_RES         209
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   442 AA;  47542 MW;  5D302DD124F2C837 CRC64;
     MSTKRNHPET IALHGGDYRS DPATNAVAVP IYRTTSYLFK DTDQAANLFA LKEFGNIYTR
     IMNPTNDVLE KRVAALEGGL ACLTVASGQT ASTFAILNVA QSGDNIVSST DLYGGTVALF
     THTLKKLGIE VRYADPADPK NFEKAIDDKT RAFYAETLPN PYLRVFPIQE VADIGKKYNI
     PLIVDNTAAP VICKPIEHGA AVVVHSLTKY IAGHGTVVGG SIVDGGNFDW TADPKRQPLF
     NEPDASYGGA VWGKVVPELT GANVAFAVRA RVTLLRDIGA ALSPDNAFGV IQGLETVALR
     MKQHCSNAEK VVEFLKNHDE VTKVIYPTEH DKNIADRAEK YLKGGKGGLV GIELKGGLDA
     GKKFIDSLKL LYHVANIGDA RSLAIHPAST THSQLTPEEQ LKAGVTPGYV RLAIGIEHVD
     DIIEDIEQAL NKSSKGTLKA VS
//
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