ID   B4DU60_HUMAN            Unreviewed;       302 AA.
AC   B4DU60;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   SubName: Full=cDNA FLJ51306, highly similar to Homo sapiens citrate lyase beta like (CLYBL), transcript variant 2, mRNA {ECO:0000313|EMBL:BAG62222.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG62222.1};
RN   [1] {ECO:0000313|EMBL:BAG62222.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Prostate {ECO:0000313|EMBL:BAG62222.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; AK300510; BAG62222.1; -; mRNA.
DR   AlphaFoldDB; B4DU60; -.
DR   MaxQB; B4DU60; -.
DR   PeptideAtlas; B4DU60; -.
DR   ProteomicsDB; 5153; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 2.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR040186; Citramalyl-CoA_lyase.
DR   InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR11105:SF0; CITRAMALYL-COA LYASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11105; CITRATE LYASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF03328; HpcH_HpaI; 2.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 2.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   2: Evidence at transcript level;
KW   Lyase {ECO:0000313|EMBL:BAG62222.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2}.
FT   DOMAIN          46..147
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   DOMAIN          163..240
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         172
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   302 AA;  32853 MW;  41E27A0FB163EF07 CRC64;
     MALRLLRRAA RGAAAAALLR LKASLAADIP RLGYSSSSHH KYIPRRAVLY VPGNDEKKIK
     KIPSLNVDCA VLDCEDGVAA NKKNEARLRI VKTLEDIDLG PTEKCVRVNS VSSGLAEEDL
     ETLLQSRVLP SSLMLPKVES PEEIQWAVCE ETLKVGPQVG LFLDAVVFGG EDFRASIGAT
     SSKETLDILY ARQKIVVIAK AFGLQAIDLV YIDFRDGAGL LRQSREGAAM GFTGKQVIHP
     NQIAVVQEQF SPSPEKIKWA EELIAAFKEH QQLGKTVSCS ASQAGVQWRD LGSLQPPPPG
     FK
//