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Database: UniProt
Entry: B3EN72_CHLPB
LinkDB: B3EN72_CHLPB
Original site: B3EN72_CHLPB 
ID   B3EN72_CHLPB            Unreviewed;       410 AA.
AC   B3EN72;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase {ECO:0000313|EMBL:ACE03602.1};
DE            EC=2.5.1.49 {ECO:0000313|EMBL:ACE03602.1};
GN   OrderedLocusNames=Cphamn1_0644 {ECO:0000313|EMBL:ACE03602.1};
OS   Chlorobium phaeobacteroides (strain BS1).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=331678 {ECO:0000313|EMBL:ACE03602.1};
RN   [1] {ECO:0000313|EMBL:ACE03602.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS1 {ECO:0000313|EMBL:ACE03602.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA   Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL   Submitted (JUN-2008) 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}.
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DR   EMBL; CP001101; ACE03602.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3EN72; -.
DR   STRING; 331678.Cphamn1_0644; -.
DR   KEGG; cpb:Cphamn1_0644; -.
DR   eggNOG; COG2873; Bacteria.
DR   HOGENOM; CLU_018986_4_0_10; -.
DR   OrthoDB; 9803729at2; -.
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   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   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:ACE03602.1}.
FT   MOD_RES         205
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   410 AA;  45115 MW;  BC7E3835B00699FD CRC64;
     MKGFTTKVLH TRYPKKDVHG ALRPPLYDSV AFEFENASAI QQAFEGKLPA HTYSRISNPT
     VEDFETKMRA LCDARGVIAV SSGMAAITNV MLALCSAGSN IVSSRHLFGN TVSLFEKTLG
     DWGLEVRYAD MNNPGSIESM IDEHTRAVYL ESITNPQLEV ADIAMVSRCA EKAGVPLVLD
     GTLTTPYLFR SRDYNVAVEV ISTTKYISGG ATGVGGVIID NGLFDWSASA KISPFIDRYG
     PFAFLAKLRR EVFRNCGSCM APHHAWMNTL GLETLALRIR QSCDNAREIA RFLAEQPKVK
     AVNYPGLPES GSHAIAAAQF KKGYGGLLAF ELENKDQCFR FIDSLGIIRN ATNLNDNKSL
     IIHPASTIFG EYSDEERHGM DISDNMLRLS VGIEDREDLL DDLQKGLENI
//
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