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Database: UniProt
Entry: D0GIV0_9FUSO
LinkDB: D0GIV0_9FUSO
Original site: D0GIV0_9FUSO 
ID   D0GIV0_9FUSO            Unreviewed;       379 AA.
AC   D0GIV0;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Cystathionine beta-lyase MetC {ECO:0000313|EMBL:EEY35976.1};
DE            EC=4.4.1.8 {ECO:0000313|EMBL:EEY35976.1};
GN   Name=metC {ECO:0000313|EMBL:EEY35976.1};
GN   ORFNames=HMPREF0554_0148 {ECO:0000313|EMBL:EEY35976.1};
OS   Pseudoleptotrichia goodfellowii F0264.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC   Pseudoleptotrichia.
OX   NCBI_TaxID=596323 {ECO:0000313|EMBL:EEY35976.1, ECO:0000313|Proteomes:UP000004226};
RN   [1] {ECO:0000313|EMBL:EEY35976.1, ECO:0000313|Proteomes:UP000004226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0264 {ECO:0000313|EMBL:EEY35976.1,
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:EEY35976.1}.
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DR   EMBL; ADAD01000029; EEY35976.1; -; Genomic_DNA.
DR   RefSeq; WP_006806381.1; NZ_ADAD01000029.1.
DR   AlphaFoldDB; D0GIV0; -.
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:SF15; CYSTATHIONINE GAMMA-LYASE; 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:EEY35976.1};
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   379 AA;  42130 MW;  C195BE8F508D1B50 CRC64;
     MKFGTKIIHG YNMIDESTGA SSISICQAST FHQSNIDDDQ KYTYSRFGNP TREALEEAIA
     CLEKGRYGLA FSSGMAAITA VLLSFSHGDH IVMCKDVYGG AFQLANEVFP RFGIEVTFVD
     ETNLDEWEKA IKENTKAFYM ETPSNPLLKI TDIKGVVNIA KKHKLLTIID NTFMTPQYQN
     PIPLGVDIVI HSATKFLNGH SDVVLGMIVT DAEDIYKELK KQQIVLGALP GVEECWLLMR
     GMKTMEIRMK KSSKTALKIA EYLEKHPKVE KVYYPGLKSH EGYETNKKQS LSGGAVLSFD
     LGCCEKVKKF FKEVKYPIVA VSLGGVESIL SYPVKMSHAC VPEEERLKMG VTSGLVRLSV
     GIEDAEDLIE DIEKALQSI
//
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