ID M9RYH9_9RHOB Unreviewed; 287 AA.
AC M9RYH9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Citrate lyase subunit beta {ECO:0000313|EMBL:AGI74905.1};
DE EC=4.1.3.34 {ECO:0000313|EMBL:AGI74905.1};
DE EC=4.1.3.6 {ECO:0000313|EMBL:AGI74905.1};
GN Name=citE {ECO:0000313|EMBL:AGI74905.1};
GN ORFNames=OA238_160p0990 {ECO:0000313|EMBL:AGI74905.1};
OS Octadecabacter arcticus 238.
OG Plasmid pOA238_160 {ECO:0000313|EMBL:AGI74905.1,
OG ECO:0000313|Proteomes:UP000004688}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Octadecabacter.
OX NCBI_TaxID=391616 {ECO:0000313|EMBL:AGI74905.1, ECO:0000313|Proteomes:UP000004688};
RN [1] {ECO:0000313|EMBL:AGI74905.1, ECO:0000313|Proteomes:UP000004688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=238 {ECO:0000313|EMBL:AGI74905.1,
RC ECO:0000313|Proteomes:UP000004688};
RC PLASMID=Plasmid pOA238_160 {ECO:0000313|Proteomes:UP000004688};
RX PubMed=23671678;
RA Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA Brinkhoff T., Simon M., Daniel R.;
RT "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT Plasticity and a New Type of Xanthorhodopsin.";
RL PLoS ONE 8:E63422-E63422(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC {ECO:0000256|ARBA:ARBA00005568}.
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DR EMBL; CP003744; AGI74905.1; -; Genomic_DNA.
DR AlphaFoldDB; M9RYH9; -.
DR KEGG; oar:OA238_160p0990; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_1_5; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000004688; Plasmid pOA238_160.
DR GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0008816; F:citryl-CoA lyase activity; IEA:UniProtKB-EC.
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:SF0; HPCH_HPAI DOMAIN-CONTAINING PROTEIN; 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 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AGI74905.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW Plasmid {ECO:0000313|EMBL:AGI74905.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004688}.
FT DOMAIN 5..223
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 287 AA; 31288 MW; 3781C09E22B42FF8 CRC64;
MSSFRSFLFT PANHVRHAEK VFTIGADVAI LDLEDAVAVN EKKEARNKAA EALQRPRCCQ
AYVRVNAMDT EFCLDDLEGV VGPALDGVML PKVESAASLL AADWILTQLE RRAGITIGSI
DLLPIIETGA GLMALEEIAK CGSRIRRLAF GAGDFTFDMN MIWTADEREL DYARSRLVAL
SRATGLEAPI DTIWVDIPNL DGLRASAETA LQMGFQGKLC IHPTQVPVVN DAFTPSDEAV
AYARKVVDAF TEAEAAGSAA LLVDGKFIDY PFVYRAQRTL KMVKDMA
//
