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Database: UniProt
Entry: K4G0J1_CALMI
LinkDB: K4G0J1_CALMI
Original site: K4G0J1_CALMI 
ID   K4G0J1_CALMI            Unreviewed;       400 AA.
AC   K4G0J1;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Cystathionine gamma-lyase {ECO:0000256|ARBA:ARBA00017343};
DE            EC=4.4.1.1 {ECO:0000256|ARBA:ARBA00012085};
DE   AltName: Full=Cysteine-protein sulfhydrase {ECO:0000256|ARBA:ARBA00031772};
DE   AltName: Full=Gamma-cystathionase {ECO:0000256|ARBA:ARBA00029853};
GN   Name=cth {ECO:0000313|Ensembl:ENSCMIP00000001857.1};
OS   Callorhinchus milii (Ghost shark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX   NCBI_TaxID=7868 {ECO:0000313|EMBL:AFK11356.1};
RN   [1] {ECO:0000313|Proteomes:UP000314986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17185593; DOI=10.1126/science.1130708;
RA   Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA   Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA   Brenner S.;
RT   "Ancient noncoding elements conserved in the human genome.";
RL   Science 314:1892-1892(2006).
RN   [2] {ECO:0000313|Proteomes:UP000314986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17407382;
RA   Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA   Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA   Brenner S.;
RT   "Survey sequencing and comparative analysis of the elephant shark
RT   (Callorhinchus milii) genome.";
RL   PLoS Biol. 5:E101-E101(2007).
RN   [3] {ECO:0000313|EMBL:AFK11356.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver {ECO:0000313|EMBL:AFK11356.1};
RX   PubMed=23056606;
RA   Tan Y.Y., Kodzius R., Tay B.H., Tay A., Brenner S., Venkatesh B.;
RT   "Sequencing and Analysis of Full-Length cDNAs, 5'-ESTs and 3'-ESTs from a
RT   Cartilaginous Fish, the Elephant Shark (Callorhinchus milii).";
RL   PLoS ONE 7:E47174-E47174(2012).
RN   [4] {ECO:0000313|Proteomes:UP000314986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24402279; DOI=10.1038/nature12826;
RG   International Elephant Shark Genome Sequencing Consortium;
RA   Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA   Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA   Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA   Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA   Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA   Wilson R.K., Brenner S., Warren W.C.;
RT   "Elephant shark genome provides unique insights into gnathostome
RT   evolution.";
RL   Nature 505:174-179(2014).
RN   [5] {ECO:0000313|Ensembl:ENSCMIP00000001857.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU362118};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-homocysteine and L-serine: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00005038}.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC       {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR   EMBL; JX053128; AFK11356.1; -; mRNA.
DR   RefSeq; NP_001279568.1; NM_001292639.1.
DR   Ensembl; ENSCMIT00000001929.1; ENSCMIP00000001857.1; ENSCMIG00000001111.1.
DR   GeneID; 103189141; -.
DR   KEGG; cmk:103189141; -.
DR   CTD; 1491; -.
DR   GeneTree; ENSGT00390000000312; -.
DR   OrthoDB; 6018at2759; -.
DR   UniPathway; UPA00136; UER00202.
DR   Proteomes; UP000314986; Unassembled WGS sequence.
DR   GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:UniProtKB-EC.
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; IEA:InterPro.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-UniPathway.
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   2: Evidence at transcript level;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW   Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR001434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000314986}.
FT   MOD_RES         209
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ   SEQUENCE   400 AA;  43786 MW;  4C034F9F83A1EB41 CRC64;
     MNGSGSGFLP PFEHFDTDAL HVGQEPEQWK CMALVPMISL STTFKQPAPA QHVGFEYSRS
     GNPTRNCLEK VVAALDGAKH SLAFASGLAA TVTITHLLKT GDGIVCFSDV YGGTNRYFRQ
     IATELGLQIS FVDCETLSSL ETAIKPNTKL VWIESPSNPL MKVSDIAACA KIVHKHEGVI
     LVVDNTFMSA YFQRPLALGA DMCMYSATKY MNGHSDVVMG LVSMNREDLY ERMKFLQNAL
     GAVPSPFDCY LCNRGLKTLS LRMKQHFKSG LMAARFLEAN PRVEKVLFPG LPSHPQYELL
     KRQCSGCSGM ISFYIKGGLE NSKIFLQSLK IFALAESLGG YESLAEHPAL MTHASVLAED
     REALGISDTL IRLSVGLENE EDLIADLDQA LKAAVPESQM
//
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