ID C1FPA3_CLOBJ Unreviewed; 426 AA.
AC C1FPA3;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase family protein {ECO:0000313|EMBL:ACO84852.1};
GN OrderedLocusNames=CLM_2092 {ECO:0000313|EMBL:ACO84852.1};
OS Clostridium botulinum (strain Kyoto / Type A2).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536232 {ECO:0000313|EMBL:ACO84852.1, ECO:0000313|Proteomes:UP000001374};
RN [1] {ECO:0000313|EMBL:ACO84852.1, ECO:0000313|Proteomes:UP000001374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyoto / Type A2 {ECO:0000313|Proteomes:UP000001374};
RA Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL Submitted (OCT-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; CP001581; ACO84852.1; -; Genomic_DNA.
DR RefSeq; WP_012704449.1; NC_012563.1.
DR AlphaFoldDB; C1FPA3; -.
DR KEGG; cby:CLM_2092; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_2_9; -.
DR Proteomes; UP000001374; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; 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:SF3; O-ACETYLHOMOSERINE SULFHYDRYLASE; 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:ACO84852.1}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 426 AA; 46928 MW; 64F66EE5164A3E65 CRC64;
MSIKNWNTET ICIQGGYTPK SGEPRILPII QSTTYKYDDP DKVANLFDLK EEGHMYTRIS
NPTVAAFEEK IAQLEGGVGA VAVSSGQSAT TLAVLNICSA GDHILASSNL YGGTFTLISS
TLKKLGIETT FVSPEASEEE ILKLAKDNTK MVLGETIGNP SVNILDFHKF SNVARKIEVP
FLVDNTLMTP YLCKPFEYGA DIVIHSATKY IDGHATSVGG VVIDGGNFNW RNGKFPSLVD
KDPTYHGISY TEEFKNLAYI TKLRVNLLRD LGTCLSPFNA FLFNLGLETL HLRMERHSEN
ALKLAQFLQE HDKITWVKYP LLKGDKSYKN AKKYLNSGAS GMLTFGIKGG TDQAKEFIKS
LKLASLVIHI GDARTSVLHP SSTTHRQLSY EEQIASGVTE DLIRVSVGIE YIGDIIKDFK
EALSKI
//