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Database: UniProt
Entry: Q1YJN0_AURMS
LinkDB: Q1YJN0_AURMS
Original site: Q1YJN0_AURMS 
ID   Q1YJN0_AURMS            Unreviewed;       262 AA.
AC   Q1YJN0;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   SubName: Full=Putative aldolase {ECO:0000313|EMBL:EAS50843.1};
GN   ORFNames=SI859A1_00969 {ECO:0000313|EMBL:EAS50843.1};
OS   Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Aurantimonadaceae; Aurantimonas.
OX   NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS50843.1, ECO:0000313|Proteomes:UP000000321};
RN   [1] {ECO:0000313|EMBL:EAS50843.1, ECO:0000313|Proteomes:UP000000321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS50843.1,
RC   ECO:0000313|Proteomes:UP000000321};
RX   PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA   Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA   McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT   "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT   Aurantimonas sp. strain SI85-9A1.";
RL   Appl. Environ. Microbiol. 74:2646-2658(2008).
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:EAS50843.1}.
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DR   EMBL; AAPJ01000002; EAS50843.1; -; Genomic_DNA.
DR   RefSeq; WP_009208832.1; NZ_CH672387.1.
DR   AlphaFoldDB; Q1YJN0; -.
DR   HOGENOM; CLU_059964_1_0_5; -.
DR   OrthoDB; 9802624at2; -.
DR   BioCyc; AURANTIMONAS:SI859A1_00969-MONOMER; -.
DR   Proteomes; UP000000321; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR   PANTHER; PTHR30502:SF0; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000321}.
FT   DOMAIN          23..247
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
SQ   SEQUENCE   262 AA;  27439 MW;  F70FBC2DCBCE53B3 CRC64;
     MAHPVTAREN RLKTRVAAGE KSFGVWLQSA NATTAEIVGL VGFDFVIIDQ EHGTGDIQSA
     IDMMRALNGT PTTAIIRVPA ADPAYLKRIV DAGAEAVLVP MVNSAAEAKS VVDACLYTPF
     GQRGNAAAVV RGSRYGLVPD YVATAHERLL VIPQIETVEA VANAEAIASV PGVDMVFIGP
     ADLSGSAGMP DQTGAPEVER LIAEAEAAVR RAGKPLATVP RQGRSWQQLL GEGYAAVASG
     SDIAWLRDAA LAQAKEWHDF AG
//
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