ID   V4IX29_9GAMM            Unreviewed;       345 AA.
AC   V4IX29;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Aldolase {ECO:0000313|EMBL:ESQ14922.1};
DE   Flags: Fragment;
GN   ORFNames=N838_10325 {ECO:0000313|EMBL:ESQ14922.1};
OS   Thiohalocapsa sp. PB-PSB1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiohalocapsa.
OX   NCBI_TaxID=1385625 {ECO:0000313|EMBL:ESQ14922.1, ECO:0000313|Proteomes:UP000017935};
RN   [1] {ECO:0000313|EMBL:ESQ14922.1, ECO:0000313|Proteomes:UP000017935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilbanks E.G., Jaekel U., Salman V., Humphrey P.T., Eisen J.A.,
RA   Facciotti M.T., Buckley D.H., Zinder S.H., Druschel G.K., Fike D.A.,
RA   Orphan V.J.;
RT   "A sulfurous symbiosis: microscale sulfur cycling in the pink berry
RT   consortia of the Sippewissett salt marsh.";
RL   Submitted (AUG-2013) 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:ESQ14922.1}.
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DR   EMBL; AVFR01000517; ESQ14922.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4IX29; -.
DR   Proteomes; UP000017935; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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   4: Predicted;
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:UP000017935}.
FT   DOMAIN          56..275
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
FT   BINDING         96
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"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT   BINDING         188
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT   NON_TER         345
FT                   /evidence="ECO:0000313|EMBL:ESQ14922.1"
SQ   SEQUENCE   345 AA;  38002 MW;  A6F8ACC80C79CD35 CRC64;
     MEVDDMKLPL NFYKPMAIGA PMPMRELPLR AERVVHFFPP HLEKIRARLP DTARKVDVLC
     GNLEDAIPID AKEAARAGFI EGVNALEPGD TAIWVRVNCL NSPWVLDDIE QIVREAGNRL
     DVVMIPKVEG PWDIHFVDQY LALLEARHGV QKPILIHALL ETAQGVMNVE QIAAASPRMH
     GMSLGPADLA ASRGMKTTRV GGGHPRYGVL ADPSEAEGDQ RAFVQQDLWH YTLARMVDAC
     VAHGLRAFYG PFGDIKDEAG CEAQFRNAFL MGCTGAWSLA PNQIPIALRV FSPEVKEVLF
     AKRILEAMPD GSGVAMIDGK MQDDATWKQA KVMVDLAQLV ARKDP
//