ID A5CTP8_CLAM3 Unreviewed; 431 AA.
AC A5CTP8;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=O-acetylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:CAN02478.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:CAN02478.1};
GN OrderedLocusNames=CMM_2400 {ECO:0000313|EMBL:CAN02478.1};
OS Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Clavibacter.
OX NCBI_TaxID=443906 {ECO:0000313|EMBL:CAN02478.1, ECO:0000313|Proteomes:UP000001564};
RN [1] {ECO:0000313|EMBL:CAN02478.1, ECO:0000313|Proteomes:UP000001564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 382 {ECO:0000313|EMBL:CAN02478.1,
RC ECO:0000313|Proteomes:UP000001564};
RX PubMed=18192381; DOI=10.1128/JB.01595-07;
RA Gartemann K.H., Abt B., Bekel T., Burger A., Engemann J., Flugel M.,
RA Gaigalat L., Goesmann A., Grafen I., Kalinowski J., Kaup O., Kirchner O.,
RA Krause L., Linke B., McHardy A., Meyer F., Pohle S., Ruckert C.,
RA Schneiker S., Zellermann E.M., Puhler A., Eichenlaub R., Kaiser O.,
RA Bartels D.;
RT "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT in pathogenicity.";
RL J. Bacteriol. 190:2138-2149(2008).
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; AM711867; CAN02478.1; -; Genomic_DNA.
DR RefSeq; WP_012039089.1; NC_009480.1.
DR AlphaFoldDB; A5CTP8; -.
DR KEGG; cmi:CMM_2400; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_11; -.
DR OrthoDB; 9780685at2; -.
DR Proteomes; UP000001564; Chromosome.
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 Transferase {ECO:0000313|EMBL:CAN02478.1}.
FT MOD_RES 209
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 431 AA; 45538 MW; 3F71EF8B5B6F3263 CRC64;
MVDREYGFKT RAIHAGNIPD ATTGARALPI YQSSAFVFDD TADAAARFAL QKYGNVYSRL
SNPTVASFEE RVASLEGGLG AVATASGLSA QYITFASLAG TGDHIVASAN LYGGSITQLD
VTLRRFGVET TFVQSSDPAD YAAAITDRTK LVFAETVANP SGEIADIEGL AAVAHAAGVP
LVIDSTIATP YLNRPIEWGA DIVIHSATKF LGGHGTTLGG VVVESGLFDW ESARFPLLDQ
PVPSYGGLNW TGNFGEYAFL TRLRAEQLRD IGPALAPHSA FLLAQGVETL PYRMQAHIDN
ARAVAEWLDA DPRITAVNWA GLPAHPHHER ARKYLPTGPG SVFTFEVAGG RAVGQRFIES
VELASHLANI GDAKTLVIHP ASTTHAQLSE SQLVDAGVLP GIVRISVGIE DVADIIHDLD
QALTAATEGA K
//
