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
//