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Database: UniProt
Entry: I0QQY3_9GAMM
LinkDB: I0QQY3_9GAMM
Original site: I0QQY3_9GAMM 
ID   I0QQY3_9GAMM            Unreviewed;       386 AA.
AC   I0QQY3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=O-succinylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:EIC83706.1};
GN   ORFNames=SPM24T3_15641 {ECO:0000313|EMBL:EIC83706.1};
OS   Serratia sp. M24T3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=932213 {ECO:0000313|EMBL:EIC83706.1, ECO:0000313|Proteomes:UP000011072};
RN   [1] {ECO:0000313|EMBL:EIC83706.1, ECO:0000313|Proteomes:UP000011072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M24T3 {ECO:0000313|EMBL:EIC83706.1,
RC   ECO:0000313|Proteomes:UP000011072};
RX   PubMed=22740681; DOI=10.1128/JB.00670-12;
RA   Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT   "Draft Genome Sequence of Serratia sp. Strain M24T3, Isolated from Pinewood
RT   Disease Nematode Bursaphelenchus xylophilus.";
RL   J. Bacteriol. 194:3764-3764(2012).
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|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:EIC83706.1}.
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DR   EMBL; AJHJ01000020; EIC83706.1; -; Genomic_DNA.
DR   RefSeq; WP_009637735.1; NZ_AJHJ01000020.1.
DR   AlphaFoldDB; I0QQY3; -.
DR   STRING; 932213.SPM24T3_15641; -.
DR   PATRIC; fig|932213.3.peg.3148; -.
DR   eggNOG; COG0626; Bacteria.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000011072; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; IPR011821; O_succ_thio_ly.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR02080; O_succ_thio_ly; 1.
DR   PANTHER; PTHR11808:SF75; CYSTATHIONINE GAMMA-SYNTHASE; 1.
DR   PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 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   Lyase {ECO:0000313|EMBL:EIC83706.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         198
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   386 AA;  41659 MW;  421A7B6CE4AD4E1B CRC64;
     MTLKQGTIAV NSGLNIDQQY GGVVPSITLS TTYSFEDFNQ PRAHDYSRRG NPTRDVVQRA
     LADLEGGAGA VLTSSGMSAI HLVCTVFLKP GDLLVAPHDC YGGSYRLFDS LSKRGAYRVL
     FVDQGDPQAL QEALDQKPKL VLIETPSNPL LRVVDIKAIC DAAHQAGALA VVDNTFLSPV
     LQQPLKLGAD LVVHSCTKYL NGHSDVVAGT VISKTAEHAT ELAWWGNNIG VTGAAFDSYL
     LLRGLRTVGV RVKQQQENAL AIVAYLQKQS LVKKLYHPSL PENQGHEIAR RQQSGFGAMV
     SFEFNGDETS LRHFLKELKL FTLAESLGGV ESLISHTATM THAGMAPEAR KAAGISDSLL
     RISVGLEDSE DLIADLEHAF QSAAKR
//
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