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Database: UniProt
Entry: A0A117V1Y0_9SPHN
LinkDB: A0A117V1Y0_9SPHN
Original site: A0A117V1Y0_9SPHN 
ID   A0A117V1Y0_9SPHN        Unreviewed;       292 AA.
AC   A0A117V1Y0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Citrate lyase {ECO:0000313|EMBL:KUR75990.1};
GN   ORFNames=AQZ49_13205 {ECO:0000313|EMBL:KUR75990.1};
OS   Novosphingobium sp. FSW06-99.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1739113 {ECO:0000313|EMBL:KUR75990.1, ECO:0000313|Proteomes:UP000061032};
RN   [1] {ECO:0000313|EMBL:KUR75990.1, ECO:0000313|Proteomes:UP000061032}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSW06-99 {ECO:0000313|EMBL:KUR75990.1,
RC   ECO:0000313|Proteomes:UP000061032};
RA   Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA   Glaeser S.;
RT   "Draft genome sequence of Novosphingobium sp. FSW06-99 (=LMG 27919), a
RT   Novosphingobium acidiphilum related species isolated from a surface water
RT   sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL   Submitted (OCT-2015) 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}.
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:KUR75990.1}.
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DR   EMBL; LLZQ01000018; KUR75990.1; -; Genomic_DNA.
DR   RefSeq; WP_067616381.1; NZ_KQ954257.1.
DR   AlphaFoldDB; A0A117V1Y0; -.
DR   STRING; 1739113.AQZ49_13205; -.
DR   OrthoDB; 9800547at2; -.
DR   Proteomes; UP000061032; 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: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:KUR75990.1};
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:UP000061032}.
FT   DOMAIN          6..234
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         133
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ   SEQUENCE   292 AA;  30896 MW;  3F79A55AC9CD9CAC CRC64;
     MTSTPRSWLF IPGDSDRKLA KAQATGADAL IIDLEDAVSD ERKPIGRATT AAWLGDAANR
     GGDSQVWVRI NALDTRLWRD DLAAIIGGAP TGIMVPKAAG PDQIAQISAE LDTLEHTHGL
     TPGQTRILPL VSETARAAVT IPAYVEATLP RLAGLTWGAE DLGAALGVTR KRDPRGHWTD
     TFRWVRTQTL LVAHALEIWA IDTLHADFRD EAGLAVVAAH AAADGFAGML AIHPAQVPII
     NRAFAPDAAA LAEARAIVAA FAANPGVGAL QIDGRMIDQP HLRQARALLG LD
//
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