GenomeNet

Database: UniProt
Entry: X0PHQ2_9LACO
LinkDB: X0PHQ2_9LACO
Original site: X0PHQ2_9LACO 
ID   X0PHQ2_9LACO            Unreviewed;       437 AA.
AC   X0PHQ2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=O-acetylhomoserine (Thiol)-lyase {ECO:0000313|EMBL:KRM03788.1};
DE   SubName: Full=O-acetylhomoserine sulfhydrylase {ECO:0000313|EMBL:GAF36587.1};
GN   ORFNames=FD41_GL001034 {ECO:0000313|EMBL:KRM03788.1}, JCM14108_1560
GN   {ECO:0000313|EMBL:GAF36587.1};
OS   Lentilactobacillus farraginis DSM 18382 = JCM 14108.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lentilactobacillus.
OX   NCBI_TaxID=1423743 {ECO:0000313|EMBL:GAF36587.1, ECO:0000313|Proteomes:UP000019488};
RN   [1] {ECO:0000313|EMBL:GAF36587.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14108 {ECO:0000313|EMBL:GAF36587.1};
RA   Yuki M., Oshima K., Suda W., Kitahara M., Kitamura K., Iida T., Hattori M.,
RA   Ohkuma M.;
RT   "Draft Genome Sequences of Two Lactobacillus Strains, L. farraginis JCM
RT   14108T and L. composti JCM 14202T, Isolated from Compost of Distilled
RT   Shochu Residue.";
RL   Genome Announc. 2:e00257-14(2014).
RN   [2] {ECO:0000313|EMBL:KRM03788.1, ECO:0000313|Proteomes:UP000051966}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18382 {ECO:0000313|EMBL:KRM03788.1,
RC   ECO:0000313|Proteomes:UP000051966};
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|ARBA:ARBA00009077, 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:GAF36587.1}.
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; BAKI01000014; GAF36587.1; -; Genomic_DNA.
DR   EMBL; AZFY01000124; KRM03788.1; -; Genomic_DNA.
DR   RefSeq; WP_035179437.1; NZ_BAKI01000014.1.
DR   AlphaFoldDB; X0PHQ2; -.
DR   STRING; 1423743.FD41_GL001034; -.
DR   PATRIC; fig|1423743.5.peg.1065; -.
DR   eggNOG; COG2873; Bacteria.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000019488; Unassembled WGS sequence.
DR   Proteomes; UP000051966; 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:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; 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   Lyase {ECO:0000313|EMBL:KRM03788.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2}.
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   437 AA;  47025 MW;  4B356C22865865C6 CRC64;
     MTEENNDLHF ETLQVHAGQT VDETGSRAVP IYQTTSYVFD NPEQAAGRFG LTDPGNIYTR
     LTNPTTDVVD KRVAALENGT AGVTLATGSA AITAAILNVA GKGDEIVSAS TLYGGTFNLF
     NVTLPKLGIK THFVDPDDPA NFEAPINEHT KALYIESIGN PGINLIDFEA VAEIAHKHGI
     ILIVDNTFGT PYLVRPLDHG ADVVVHSATK FIGGHGTTMG GVIVENGKFD WKASGRYPGF
     TEPNAQYNGL VFADLGGGAF TTKVRAESLR DLGATISPFN SFLLLQGLES LSLRVERHVE
     NTKKIVNFLH NHPKVAWINY PGLEDSKYHD LAEKYFPKGV GSIFTLGLKG GEKAGKQLIE
     NLKLFSLLAN VADAKSLIIH PASTTHAQLN EEELKEAGIT PDLIRVSVGV ENADDLIADL
     SQALDKIPVE EKESVQS
//
DBGET integrated database retrieval system