ID Q7M844_WOLSU Unreviewed; 422 AA.
AC Q7M844;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=O-ACETYLHOMOSERINE (THIOL)-LYASE {ECO:0000313|EMBL:CAE10904.1};
DE EC=2.5.1.49 {ECO:0000313|EMBL:CAE10904.1};
GN Name=METY {ECO:0000313|EMBL:CAE10904.1};
GN OrderedLocusNames=WS1894 {ECO:0000313|EMBL:CAE10904.1};
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121 {ECO:0000313|Proteomes:UP000000422};
RN [1] {ECO:0000313|EMBL:CAE10904.1, ECO:0000313|Proteomes:UP000000422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 /
RC NCTC 11488 / FDC 602W {ECO:0000313|Proteomes:UP000000422};
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon JM., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
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; BX571662; CAE10904.1; -; Genomic_DNA.
DR RefSeq; WP_011139687.1; NC_005090.1.
DR AlphaFoldDB; Q7M844; -.
DR STRING; 273121.WS1894; -.
DR KEGG; wsu:WS1894; -.
DR eggNOG; COG2873; Bacteria.
DR HOGENOM; CLU_018986_4_0_7; -.
DR BRENDA; 2.5.1.49; 6642.
DR Proteomes; UP000000422; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:CAE10904.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000422};
KW Transferase {ECO:0000313|EMBL:CAE10904.1}.
FT MOD_RES 204
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 422 AA; 45867 MW; A13B95CEDE07BABD CRC64;
MHPKTLAIQA GYEKGKGEKS IAVPIYQTTA YKFDDTEHGA NLFDLKELGN IYTRIMNPTT
DVLEKRVALL EGGVAALASA SGMASIFYAV ANLAQSGENI IATTQLYGGT LNQFTHTLSR
FGIEVRFFDG NHPQEARALI DSKSRALFFE SLTNPSIDVP EIDTLAKIAD EYGIVSIVDN
TVATPAICRP IEHGVDVVVH SASKYMGGQG LAIGGVLVES ARVAEKLRGN PRYPHFNTPD
PSYHGLVYAS APLPPFVLRA RLALLRDIGA TLSPFDSWLF IQGIETLSVR MREHSLSAMK
IAHYLQNHPK VQAVYYPGLE SDKNHANAVK YFDEGMFSGL LSFEVGDFEL AQKIADSVKI
FTLATNIGDT KSIITHSAST THRQVSAEGL KKAGVTPGLV RLSIGLEDYR DLIEDLAQAI
DG
//
