ID A9BWL5_DELAS Unreviewed; 293 AA.
AC A9BWL5;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=2-dehydro-3-deoxyglucarate aldolase {ECO:0000313|EMBL:ABX36542.1};
DE EC=4.1.2.20 {ECO:0000313|EMBL:ABX36542.1};
GN OrderedLocusNames=Daci_3911 {ECO:0000313|EMBL:ABX36542.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX36542.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX36542.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC {ECO:0000256|ARBA:ARBA00005568}.
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DR EMBL; CP000884; ABX36542.1; -; Genomic_DNA.
DR AlphaFoldDB; A9BWL5; -.
DR STRING; 398578.Daci_3911; -.
DR KEGG; dac:Daci_3911; -.
DR eggNOG; COG3836; Bacteria.
DR HOGENOM; CLU_059964_1_0_4; -.
DR Proteomes; UP000000784; Chromosome.
DR GO; GO:0008672; F:2-dehydro-3-deoxyglucarate aldolase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:ABX36542.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000784}.
FT DOMAIN 27..258
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT REGION 272..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 293 AA; 30928 MW; 2C0C4BC89DE72CEB CRC64;
MNSFRRAPMS MLPANTFKRA LREARPQIGL WSTIPSPFVC EMIGGAGYDW VLLDTEHTPT
DVPLMLGQLQ AVAAALPAPG ALPVHAVVRP ACNDAVLIKR YLDLGAQSLL LPFVQNAQQA
RDAVRAMRYA PQGMRGMGGS TRAANFGRTA DYVARAADEL CLLVQVETAE ALEQIEAIAA
VDGVDGIFIG PADLSASLGY PGQARHPVVN RAIDQAIARI RACGKAPGIL MVDEARAREC
LELGAQFVAV ALDTLLLRDG LDAAAARFRK GPLAANPPGP ASTAGSYRGA PQP
//
