ID A0A0R1GKK4_9LACO Unreviewed; 406 AA.
AC A0A0R1GKK4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=O-succinylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:KRK34636.1};
GN ORFNames=FC07_GL000387 {ECO:0000313|EMBL:KRK34636.1};
OS Loigolactobacillus bifermentans DSM 20003.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=1423726 {ECO:0000313|EMBL:KRK34636.1, ECO:0000313|Proteomes:UP000051461};
RN [1] {ECO:0000313|EMBL:KRK34636.1, ECO:0000313|Proteomes:UP000051461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20003 {ECO:0000313|EMBL:KRK34636.1,
RC ECO:0000313|Proteomes:UP000051461};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRK34636.1}.
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DR EMBL; AZDA01000090; KRK34636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1GKK4; -.
DR STRING; 1423726.FC07_GL000387; -.
DR PATRIC; fig|1423726.3.peg.404; -.
DR Proteomes; UP000051461; 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF91; 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:KRK34636.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000051461}.
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 406 AA; 45069 MW; C9C58EC1C03AA696 CRC64;
MELYGLKQGG TTRQRPFYIR RGAFFILEKK KRKIKMTENR RHVSLETELA QAGNRSDEDN
TKSISAPLYF STAFRHDELN SELGPCDYSR VATPTRTILE DVLAKLEHGV QAFALSSGMA
AIQLVFSQFK TGDLIITSND LYGGSFRFFD QLTSHYGIRF ELWDGHDDAA LRKLCAEKPK
ALWIETPSNP TMKVIDIHKA AETVHEFGAQ LIVDNTFYTP LLQQPLVEGA DIVVHSATKF
LGGHNDLLAG AVMVREQKLA DELAENFITT GTNLAPFDCW LLLRSLKTLP LRLRQQEANA
QGLVKVLAAS AQVEKVLYPG HGGMISFYIN PAIDVEQFLL KLQVISFAES LGGVESLITV
PALRTHAEMP ETQRLALGIT PNLLRLSVGV EALTDLSEDL KQALAE
//
