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Database: UniProt
Entry: A0A1Z5H757_9GAMM
LinkDB: A0A1Z5H757_9GAMM
Original site: A0A1Z5H757_9GAMM 
ID   A0A1Z5H757_9GAMM        Unreviewed;       316 AA.
AC   A0A1Z5H757;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=HpcH/HpaI aldolase/citrate lyase domain-containing protein {ECO:0000259|Pfam:PF03328};
GN   ORFNames=bplSymb_SCF00506P007 {ECO:0000313|EMBL:GAW85302.1};
OS   Bathymodiolus platifrons methanotrophic gill symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=113268 {ECO:0000313|EMBL:GAW85302.1, ECO:0000313|Proteomes:UP000196430};
RN   [1] {ECO:0000313|EMBL:GAW85302.1, ECO:0000313|Proteomes:UP000196430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPD1508-B01-01 {ECO:0000313|EMBL:GAW85302.1,
RC   ECO:0000313|Proteomes:UP000196430};
RX   PubMed=28453654; DOI=10.1093/gbe/evx082;
RA   Takishita K., Takaki Y., Chikaraishi Y., Ikuta T., Ozawa G., Yoshida T.,
RA   Ohkouchi N., Fujikura K.;
RT   "Genomic Evidence that Methanotrophic Endosymbionts Likely Provide Deep-Sea
RT   Bathymodiolus Mussels with a Sterol Intermediate in Cholesterol
RT   Biosynthesis.";
RL   Genome Biol. Evol. 9:1148-1160(2017).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAW85302.1}.
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DR   EMBL; BDMN01000044; GAW85302.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5H757; -.
DR   OrthoDB; 6831788at2; -.
DR   Proteomes; UP000196430; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
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; PTHR32308:SF10; CITRATE LYASE SUBUNIT BETA; 1.
DR   PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-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|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196430}.
FT   DOMAIN          19..249
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   316 AA;  33987 MW;  03B7032E9D1832D5 CRC64;
     MSHTLYEANA QRVHRCELAV PGSNPEMFEK ALKSGVDVIF LDLEDAVAPD DKLQARKNVI
     KAINELDWAG HGITVSIRIN GLDTQYMVRD VVDLVEQCGD RIDTILIPKV GVYSDVYMVE
     SMLNQLEMQQ GLTKKIGIEC LIETALGMAN VEDIAKQGAI GGRLEALHFG VADYAASNRA
     RTTNIGGLNP DYPGDQWHFA ISRMTVACRA YGLRAIDGPF GDFKDPEGFK DAARRAAALG
     CEGKWAIHPS QIVLANEVFT PPAAEVEKAK RILVALKEAA AQGKGAAALD GRLIDAASEK
     MANNVVNTAA AIAAKA
//
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