ID B1L5K2_KORCO Unreviewed; 348 AA.
AC B1L5K2;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Cystathionine gamma-lyase {ECO:0000313|EMBL:ACB07731.1};
DE EC=4.4.1.1 {ECO:0000313|EMBL:ACB07731.1};
GN OrderedLocusNames=Kcr_0985 {ECO:0000313|EMBL:ACB07731.1};
OS Korarchaeum cryptofilum (strain OPF8).
OC Archaea; Candidatus Korarchaeota; Korarchaeum.
OX NCBI_TaxID=374847 {ECO:0000313|EMBL:ACB07731.1, ECO:0000313|Proteomes:UP000001686};
RN [1] {ECO:0000313|EMBL:ACB07731.1, ECO:0000313|Proteomes:UP000001686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF8 {ECO:0000313|Proteomes:UP000001686};
RX PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA Richardson P., Keller M., Stetter K.O.;
RT "A korarchaeal genome reveals new insights into the evolution of the
RT Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; CP000968; ACB07731.1; -; Genomic_DNA.
DR AlphaFoldDB; B1L5K2; -.
DR STRING; 374847.Kcr_0985; -.
DR EnsemblBacteria; ACB07731; ACB07731; Kcr_0985.
DR KEGG; kcr:Kcr_0985; -.
DR eggNOG; arCOG00060; Archaea.
DR HOGENOM; CLU_018986_2_0_2; -.
DR InParanoid; B1L5K2; -.
DR PhylomeDB; B1L5K2; -.
DR Proteomes; UP000001686; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IBA:GO_Central.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IEA:UniProtKB-EC.
DR GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IBA:GO_Central.
DR GO; GO:0019346; P:transsulfuration; IBA:GO_Central.
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.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:ACB07731.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001686}.
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 38439 MW; F75427B86C4D685D CRC64;
MTATFQNPLP SGKPNISRRG KELKYSREEN PTVEELERIV ASLDGYDDCL AFNSGMASIS
TLFLSRYRKR IVVNLDSYSA TVGLALRLKA MGFDIEICST DHLGECIKPG SLVFTESITN
PLLRVPDLEM LRDSCIDKGA EFIIDNTSAT PVLLKPSLFS DLSIQSATKY LSGTNDTVGG
VVSGNELSEL WEWRRVLGSI LDPFRAFLII RGVKTLELRM RRHCETALTL ARWLQDHPKV
KEVIYPGLET HKDHQIAKRL LKGFGGIISF RINGDARKFL MNLRKIKRAT SFGASISLAS
IPHGSASSNL TEDLIKASGI DGSLIRLSVG LEDPEILIED LDSSLKGI
//
