ID D5EDF5_AMICL Unreviewed; 295 AA.
AC D5EDF5;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Citrate (Pro-3S)-lyase {ECO:0000313|EMBL:ADE56587.1};
DE EC=4.1.3.6 {ECO:0000313|EMBL:ADE56587.1};
GN OrderedLocusNames=Amico_0446 {ECO:0000313|EMBL:ADE56587.1};
OS Aminobacterium colombiense (strain DSM 12261 / ALA-1).
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Aminobacterium.
OX NCBI_TaxID=572547 {ECO:0000313|EMBL:ADE56587.1, ECO:0000313|Proteomes:UP000002366};
RN [1] {ECO:0000313|EMBL:ADE56587.1, ECO:0000313|Proteomes:UP000002366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12261 / ALA-1 {ECO:0000313|Proteomes:UP000002366};
RX PubMed=21304712;
RA Chertkov O., Sikorski J., Brambilla E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Aminobacterium colombiense type strain (ALA-
RT 1).";
RL Stand. Genomic Sci. 2:280-289(2010).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; CP001997; ADE56587.1; -; Genomic_DNA.
DR AlphaFoldDB; D5EDF5; -.
DR STRING; 572547.Amico_0446; -.
DR KEGG; aco:Amico_0446; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_0_0; -.
DR Proteomes; UP000002366; Chromosome.
DR GO; GO:0008815; F:citrate (pro-3S)-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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:ADE56587.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002366}.
FT DOMAIN 5..224
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 295 AA; 31838 MW; 7D8E6541EA471F97 CRC64;
MKLRRSLLYI PGNNPAMLQS CPSLGADCVI LDLEDAVAPA HKDEARRLVA YALRCLFFDC
VEKVVRINDV STPWWELDLE EIVPAGPDVI RLPKAESVEN IRMVDNRITE LEKANGLSEG
GIELHILLES AQAVENVANL VRSCKRVKGV GLGGQDLTAD MGIRKTSSGE ELAYANGHMI
LAAKAAKIDC FDSVYTDIND GEGLLTNTRK AATMGFSGKS AIHPSQVRII NQGFYPSEDI
LSHAQDVIAA AKIARTEGRG AFSVNGKMVD GPVIRQAMNV LAQAGIPCNS EEVLP
//
