ID F5SVX2_9GAMM Unreviewed; 329 AA.
AC F5SVX2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Putative citrate lyase {ECO:0000313|EMBL:EGL55693.1};
GN ORFNames=MAMP_02687 {ECO:0000313|EMBL:EGL55693.1};
OS Methylophaga aminisulfidivorans MP.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL55693.1, ECO:0000313|Proteomes:UP000003544};
RN [1] {ECO:0000313|EMBL:EGL55693.1, ECO:0000313|Proteomes:UP000003544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544};
RX PubMed=21685284; DOI=10.1128/JB.05403-11;
RA Han G.H., Kim W., Chun J., Kim S.W.;
RT "Draft genome sequence of Methylophaga aminisulfidivorans MP T.";
RL J. Bacteriol. 193:4265-4265(2011).
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:EGL55693.1}.
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DR EMBL; AFIG01000001; EGL55693.1; -; Genomic_DNA.
DR RefSeq; WP_007145579.1; NZ_AFIG01000001.1.
DR AlphaFoldDB; F5SVX2; -.
DR STRING; 1026882.MAMP_02687; -.
DR eggNOG; COG2301; Bacteria.
DR OrthoDB; 8481499at2; -.
DR Proteomes; UP000003544; 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:EGL55693.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000003544}.
FT DOMAIN 68..243
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 87
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"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 329 AA; 37219 MW; BF4A3240748DB27F CRC64;
MTILIHPNDA LVDDISPLPL IPACEHFAGS RHTLLKAFSI QSEYGPVFDI TCDCEDGAAS
GGEIQHANMI VELLNSEHNI HHMSGIRIHG YDHSVWRQEI DILLSGARDN IRYITLPKAQ
NAHQVEVMLE YIQQASQRYN ITHPIPIHVL IETHGALNDV YKIAAMKPVQ VLDFGIMDYI
SAYQGAITDN AMHSPTQFEH ALIVRAKTEI ACAAISSGCI PSHNVTLAIK DYQQTFEDAY
RARNQFGFLR MWSVHPQQIK AIIKAMTPES EKIQLASEIL LTAQQRSWAP ISLNDKLYDK
ASYRYYWQLL QRAHLSGEKL STDVQEQFF
//
