GenomeNet

Database: UniProt
Entry: D0GPQ2_9FUSO
LinkDB: D0GPQ2_9FUSO
Original site: D0GPQ2_9FUSO 
ID   D0GPQ2_9FUSO            Unreviewed;       378 AA.
AC   D0GPQ2;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Cystathionine beta-lyase MetC {ECO:0000313|EMBL:EEY33897.1};
DE            EC=4.4.1.8 {ECO:0000313|EMBL:EEY33897.1};
GN   Name=metC {ECO:0000313|EMBL:EEY33897.1};
GN   ORFNames=HMPREF0554_0073 {ECO:0000313|EMBL:EEY33897.1};
OS   Pseudoleptotrichia goodfellowii F0264.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Pseudoleptotrichia.
OX   NCBI_TaxID=596323 {ECO:0000313|EMBL:EEY33897.1, ECO:0000313|Proteomes:UP000004226};
RN   [1] {ECO:0000313|EMBL:EEY33897.1, ECO:0000313|Proteomes:UP000004226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0264 {ECO:0000313|EMBL:EEY33897.1,
RC   ECO:0000313|Proteomes:UP000004226};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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:EEY33897.1}.
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; ADAD01000200; EEY33897.1; -; Genomic_DNA.
DR   RefSeq; WP_006808461.1; NZ_ADAD01000200.1.
DR   AlphaFoldDB; D0GPQ2; -.
DR   eggNOG; COG0626; Bacteria.
DR   Proteomes; UP000004226; Unassembled WGS sequence.
DR   GO; GO:0004121; F:cystathionine beta-lyase 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; 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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:EEY33897.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004226}.
FT   MOD_RES         195
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   378 AA;  42128 MW;  C76ECF4F99C476D9 CRC64;
     MKFETKAIHG IRKDDGKHSG WKSTINMAST AQIENFGEEQ EFEYARVSNP TRSELEKIMA
     KLENGKHAFA FSSGMAAITS LFTKFKAGDH IVLGTDIYGG TYRIMTDIFG KYNLEYTFVD
     TTDLQNIEKA VKDNTVAIFI ETPSNPLLDV TDIKGVVEIA KKYELLTITD NTFMTPYLQR
     PLDLGINIVV HSATKFLSGH HDILAGMVIV NSDELAEEVW FAQKAIGAIL SPFDSWLLMR
     SLKTLKVRIE AAQKNTLKLI EFFKNHKAVG KVYFPTEENN KGKKIHESQA TGGGAVFSFV
     LKDENKVKPF FDNLKVALSA ASLGGVETLV THPHTITHAE MPEDEKNARG ITKSLIRVAV
     GIEHIDDLIE DFKNALEK
//
DBGET integrated database retrieval system