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Database: UniProt
Entry: A0A096AG23_9MICC
LinkDB: A0A096AG23_9MICC
Original site: A0A096AG23_9MICC 
ID   A0A096AG23_9MICC        Unreviewed;       443 AA.
AC   A0A096AG23;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:KGF19899.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:KGF19899.1};
GN   ORFNames=HMPREF2128_07930 {ECO:0000313|EMBL:KGF19899.1};
OS   Pseudoglutamicibacter albus DNF00011.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Pseudoglutamicibacter.
OX   NCBI_TaxID=1401063 {ECO:0000313|EMBL:KGF19899.1, ECO:0000313|Proteomes:UP000053528};
RN   [1] {ECO:0000313|EMBL:KGF19899.1, ECO:0000313|Proteomes:UP000053528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DNF00011 {ECO:0000313|EMBL:KGF19899.1,
RC   ECO:0000313|Proteomes:UP000053528};
RA   McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JUL-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:KGF19899.1}.
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DR   EMBL; JRNH01000023; KGF19899.1; -; Genomic_DNA.
DR   RefSeq; WP_035756864.1; NZ_JRNH01000023.1.
DR   AlphaFoldDB; A0A096AG23; -.
DR   Proteomes; UP000053528; 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:UP000053528};
KW   Transferase {ECO:0000313|EMBL:KGF19899.1}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         209
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   443 AA;  47638 MW;  460CE1EBF089F696 CRC64;
     MSQQKFETRQ IHAGQTPDPT TGSQALPIHL TNAYVFPDTE AAANRFALSE LGPIYTRLGN
     PTTEVIENRM ASLEGGVGAL FVASGMAATS YAILNVAEAG DHIVASPSLY GGTQNLFKHT
     LPKLGVEVTF VEDPDDLDAW RGAIKPNTKA FFGETIGNPR QDVFDIENIA AIAHDEAGVP
     LIIDNTLATP YSLRPIEWGA DVVVHSATKY LCGHGTAMGG VIIDSGNFDY TKHPERFPGF
     NQPDESYHGI VYGRDMGVGS PLGANLSYIL KVRVQLLRDT GAAISPMNSF LIAQGLETLS
     LRVERHIENA QKVAQWLEAR DDVSATIYAG LESCPWYERG RHYAPEGVGA IVSFEIKGAE
     DNEEAARAFV DALELHSLVA NLGDVRSLVA HPSSTTHSQL SPEEKRAAGV GPGTVRLSVG
     LEHVDDIIAD LQKGFDAFHA ARA
//
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