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Database: UniProt
Entry: A0A1T1AQK0_RHOFE
LinkDB: A0A1T1AQK0_RHOFE
Original site: A0A1T1AQK0_RHOFE 
ID   A0A1T1AQK0_RHOFE        Unreviewed;       353 AA.
AC   A0A1T1AQK0;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=CoA ester lyase {ECO:0000313|EMBL:OOV06248.1};
GN   ORFNames=RF819_05470 {ECO:0000313|EMBL:OOV06248.1};
OS   Rhodoferax fermentans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=28066 {ECO:0000313|EMBL:OOV06248.1, ECO:0000313|Proteomes:UP000190750};
RN   [1] {ECO:0000313|EMBL:OOV06248.1, ECO:0000313|Proteomes:UP000190750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7819 {ECO:0000313|EMBL:OOV06248.1,
RC   ECO:0000313|Proteomes:UP000190750};
RA   Kim Y.J., Farh M.E.-A., Yang D.-C.;
RT   "Genome sequencing of Rhodoferax fermentans JCM 7819.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OOV06248.1}.
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DR   EMBL; MTJN01000002; OOV06248.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T1AQK0; -.
DR   STRING; 28066.RF819_05470; -.
DR   Proteomes; UP000190750; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.140.960; -; 1.
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   Lyase {ECO:0000313|EMBL:OOV06248.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190750}.
FT   DOMAIN          42..240
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         166
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         192
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   353 AA;  38012 MW;  7CFFA9AE7B00CC94 CRC64;
     MNHTNVTHPR HVLLGAAVAA PLPVCDHYCG VESRMRKALA LQAEMTEEFG TCVFDVTLDC
     EDGAPVGGEK DHAFMVSALV NQGLVATKNK AINGARRVAV RVHPVDHPAF EQDVQIVVGE
     AGAAWSHLML PKVDGVADVD RAARVIDAAL ASSNRAQALP LHVLIESPLA VQQVAAIAAH
     PRVQSLSFGL MDFVSAHGGA IPASAMAVAE PGAQTTYDQF SHPLVVRAKL EVSAACHAFG
     KVPSHCVVTE FKRPDVVQAA ALRASRELGY TRMWSIHPDQ IRPILAAFTP AQSEVEQASH
     IICAAHAADW APISVAGKLH DRASYRYYWQ VLEKAYQTAQ LDHQDPAFPY FVL
//
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