ID   A7H124_CAMC5            Unreviewed;       380 AA.
AC   A7H124;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Cystathionine-beta-lyase {ECO:0000313|EMBL:EAT99518.1};
DE            EC=4.4.1.8 {ECO:0000313|EMBL:EAT99518.1};
GN   Name=metC {ECO:0000313|EMBL:EAT99518.1};
GN   ORFNames=CCV52592_1762 {ECO:0000313|EMBL:EAT99518.1};
OS   Campylobacter curvus (strain 525.92).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360105 {ECO:0000313|EMBL:EAT99518.1, ECO:0000313|Proteomes:UP000006380};
RN   [1] {ECO:0000313|Proteomes:UP000006380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=525.92 {ECO:0000313|Proteomes:UP000006380};
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT   feces.";
RL   Submitted (JUL-2007) 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|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; CP000767; EAT99518.1; -; Genomic_DNA.
DR   RefSeq; WP_011992863.1; NC_009715.2.
DR   AlphaFoldDB; A7H124; -.
DR   STRING; 360105.CCV52592_1762; -.
DR   KEGG; ccv:CCV52592_1762; -.
DR   HOGENOM; CLU_018986_2_0_7; -.
DR   OrthoDB; 9805807at2; -.
DR   Proteomes; UP000006380; Chromosome.
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:SF92; 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:EAT99518.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006380}.
FT   MOD_RES         194
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   380 AA;  41818 MW;  11525C463E336A20 CRC64;
     MKIDTLIVKG IEAKDNPYNA VVPPIVLSST FAQEGLGEFG EFAYSRSANP TKKAFEELFA
     KFEGSKYSFA LASGMAATTA VFNLLKSGDK VLLNNNVYGG TYRYASGIFK NQGISYELVD
     DLNLIEEDDI TDDVKMVFIE TPSNPLLRVT DIKRIVNLAH KKGALVVVDN TFLTPYYQRL
     LPLGVDIVVY SATKYIGGHA DVIAGIVSTN DDALADRIAF MKNTLGATLS PTDAYYLIRG
     LKTLSVRFDR QTQNTHKIVE FLKSNSAVRT VYYAGSYSEF EKRAQEAQAS DIGAVISLEL
     AEGYDYEKFA KSLHLFDLAV SLGGVESLIC HPASMTHESY PKELQEKIGI SQNLLRLAIG
     IENADDLIDD LKQALIKAKK
//