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Database: UniProt
Entry: I0I301_CALAS
LinkDB: I0I301_CALAS
Original site: I0I301_CALAS 
ID   I0I301_CALAS            Unreviewed;       407 AA.
AC   I0I301;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:BAL99638.1};
GN   Name=metC {ECO:0000313|EMBL:BAL99638.1};
GN   OrderedLocusNames=CLDAP_15990 {ECO:0000313|EMBL:BAL99638.1};
OS   Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS   STL-6-O1).
OC   Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC   Caldilinea.
OX   NCBI_TaxID=926550 {ECO:0000313|EMBL:BAL99638.1, ECO:0000313|Proteomes:UP000007880};
RN   [1] {ECO:0000313|EMBL:BAL99638.1, ECO:0000313|Proteomes:UP000007880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC   {ECO:0000313|Proteomes:UP000007880};
RA   Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA   Hanada S., Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT   102666).";
RL   Submitted (FEB-2012) 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}.
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DR   EMBL; AP012337; BAL99638.1; -; Genomic_DNA.
DR   RefSeq; WP_014432877.1; NC_017079.1.
DR   AlphaFoldDB; I0I301; -.
DR   STRING; 926550.CLDAP_15990; -.
DR   KEGG; cap:CLDAP_15990; -.
DR   PATRIC; fig|926550.5.peg.1793; -.
DR   eggNOG; COG0626; Bacteria.
DR   HOGENOM; CLU_018986_2_0_0; -.
DR   OrthoDB; 9780685at2; -.
DR   Proteomes; UP000007880; Chromosome.
DR   GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; 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; IPR044639; CGS1/2.
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; PTHR43379; CYSTATHIONINE GAMMA-SYNTHASE; 1.
DR   PANTHER; PTHR43379:SF1; CYSTATHIONINE GAMMA-SYNTHASE 1, CHLOROPLASTIC-RELATED; 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:BAL99638.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007880}.
FT   MOD_RES         223
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   407 AA;  44849 MW;  9BA979EDDC68FEB0 CRC64;
     MQQTQSSTDA IRSSTITSTQ AVHAGEQRFR SHHSLTVPIV QTAVYTFDTT EALIRYTEER
     LFWNEPEREE YGRYGNPTVR ALEAKIAELE GAQDAIVVSS GMGAVTSTLL LLLQPGQHFI
     LTDNCYLSTL EFCQNFLKRY GIECTLVPFG DYDAIEAAVC PQTRLIFSES PTNPFVRCLD
     FERLVSIARC HHLLTVVDST FATPYNLRPL AFGVDLVIHS LTKYLAGHND AMAGVVAGRY
     DLTTPLRQMQ GLLGNIAAPQ TAYLILRGIK TLALRMERQN ASGLAVARFL EGHPKVRRVW
     YPFLESHPDY AVARATLRGG GGVVSFEIEG DAGRAHRFID ALRIPVIGPS LGGVESIVSP
     LALMGYANLS PEERLALGIR DELVRLCIGI EDTENLIADL AQALDQI
//
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