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Database: UniProt
Entry: A7RLV7_NEMVE
LinkDB: A7RLV7_NEMVE
Original site: A7RLV7_NEMVE 
ID   A7RLV7_NEMVE            Unreviewed;       285 AA.
AC   A7RLV7;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=HpcH/HpaI aldolase/citrate lyase domain-containing protein {ECO:0000259|Pfam:PF03328};
GN   ORFNames=NEMVEDRAFT_v1g179528 {ECO:0000313|EMBL:EDO47490.1};
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO47490.1, ECO:0000313|Proteomes:UP000001593};
RN   [1] {ECO:0000313|EMBL:EDO47490.1, ECO:0000313|Proteomes:UP000001593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; DS469519; EDO47490.1; -; Genomic_DNA.
DR   RefSeq; XP_001639553.1; XM_001639503.1.
DR   AlphaFoldDB; A7RLV7; -.
DR   STRING; 45351.A7RLV7; -.
DR   EnsemblMetazoa; EDO47490; EDO47490; NEMVEDRAFT_v1g179528.
DR   eggNOG; ENOG502QQPK; Eukaryota.
DR   HOGENOM; CLU_044864_1_1_1; -.
DR   InParanoid; A7RLV7; -.
DR   OMA; AWLFCPA; -.
DR   PhylomeDB; A7RLV7; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
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; 1.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001593}.
FT   DOMAIN          2..220
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         152
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   285 AA;  31381 MW;  99C66556DD6BA3A7 CRC64;
     MPGNDEKKIR KATGLDADCV VLDCEDAVAI NRKEEARRTI SELLAVLSFG RSEVCVRVNS
     VSSGLAEDDL NAVFNAKTLP QTIVVPKMDS VAELKWVNDK IGRLMKEKKQ KIGLITQAES
     AISLLNLREV CEYGTSEQRN FALQAIIFGS DDFLVSIGGT RTKDAKELLF ARQYVVVHAK
     AFGLQAIDLV DIDFKDLIGL KSQSEEGARM GFTGKQIIHP GQIDIVNKAF SPPPEKIKWA
     KDLLSAFEEQ EKQGKGAMSF QGDMIDMPLV LQARAIVRLA DVLQS
//
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