ID A0A1M6F250_9PROT Unreviewed; 262 AA.
AC A0A1M6F250;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Citrate lyase subunit beta / citryl-CoA lyase {ECO:0000313|EMBL:SHI91763.1};
GN ORFNames=SAMN02745194_01368 {ECO:0000313|EMBL:SHI91763.1};
OS Roseomonas rosea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Roseomonas.
OX NCBI_TaxID=198092 {ECO:0000313|EMBL:SHI91763.1, ECO:0000313|Proteomes:UP000184387};
RN [1] {ECO:0000313|EMBL:SHI91763.1, ECO:0000313|Proteomes:UP000184387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14916 {ECO:0000313|EMBL:SHI91763.1,
RC ECO:0000313|Proteomes:UP000184387};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; FQZF01000006; SHI91763.1; -; Genomic_DNA.
DR RefSeq; WP_073132921.1; NZ_FQZF01000006.1.
DR AlphaFoldDB; A0A1M6F250; -.
DR STRING; 198092.SAMN02745194_01368; -.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000184387; 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; 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 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:SHI91763.1};
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:UP000184387}.
FT DOMAIN 8..205
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 262 AA; 26716 MW; E625F7D0756B06E9 CRC64;
MTAPIAPLFV PGNRPERFAK AAASGADAVI IDLEDAVAPE DKAAARRAAA EARPEGVPLF
VRLNAAGTPW HAEDLAALSG SPAGILLPKA EDPAALAAIR AAIGPDRPLV ALVESVRGLA
AARELARGAS RLAFGSIDYA ADLGCAHTRE ALLAARSELV FASRLAGIDA PMDGVTATIG
DDTLTEEDAR HAAGLGFGGK LLIHPRQVAA ALRGFAPEAK EVEWARGVLA AGGDGAVQVG
GMMIDAPVRI RAERILARAG KG
//
