ID Q1LTT9_BAUCH Unreviewed; 387 AA.
AC Q1LTT9;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=O-succinylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:ABF14162.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:ABF14162.1};
GN Name=metB {ECO:0000313|EMBL:ABF14162.1};
GN OrderedLocusNames=BCI_0163 {ECO:0000313|EMBL:ABF14162.1};
OS Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Baumannia.
OX NCBI_TaxID=374463 {ECO:0000313|EMBL:ABF14162.1, ECO:0000313|Proteomes:UP000002427};
RN [1] {ECO:0000313|EMBL:ABF14162.1, ECO:0000313|Proteomes:UP000002427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hc {ECO:0000313|EMBL:ABF14162.1};
RX PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT sharpshooters.";
RL PLoS Biol. 4:1079-1092(2006).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000238; ABF14162.1; -; Genomic_DNA.
DR RefSeq; WP_011520358.1; NC_007984.1.
DR AlphaFoldDB; Q1LTT9; -.
DR STRING; 374463.BCI_0163; -.
DR KEGG; bci:BCI_0163; -.
DR HOGENOM; CLU_018986_2_0_6; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000002427; Chromosome.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
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:ABF14162.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002427};
KW Transferase {ECO:0000313|EMBL:ABF14162.1}.
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 387 AA; 41800 MW; 24AA27FB4D7579D1 CRC64;
MKHKQATIAV RSGLNNDEQF GCVVPPITLS STYNFIAFNQ PRTHDYSRRR NPTRDIVHSV
LAGLEGGAGA VMTSSGMSAI HLVCTALLKP GDLLVAPYDC YGGSYRLFES FSKRGVYKVQ
FLDQGNKTNL AVILASKPKL VLIETPSNPL LRVVDIAAIC STAHQVGAQC VVDNTFMSPV
LQQPIALGAD LVVHSCTKYL NGHSDVMAGV VIAKEAAVAD KLAWWGNNIG VTGGTFDSYL
LLRGIRTLNL RILQQQSNAQ AIVTYLQQHH QIKKLYYPSL PGHPGHEIAC RQQNGFGAML
SFELDGNEIT LRRFLAALEL FTLAESLGGV ESLISHAATM THAGMNAIAR AKAGISDNLL
RISVGIEDSQ DLISDLAHAL QAAKRLT
//
