ID A0A177H9T0_9RHOB Unreviewed; 303 AA.
AC A0A177H9T0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=L-2-keto-3-deoxyarabonate dehydratase {ECO:0000313|EMBL:OAH07017.1};
DE EC=4.2.1.43 {ECO:0000313|EMBL:OAH07017.1};
GN Name=araD {ECO:0000313|EMBL:OAH07017.1};
GN ORFNames=pfor_22c2553 {ECO:0000313|EMBL:OAH07017.1};
OS Rhodobacteraceae bacterium SB2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1689867 {ECO:0000313|EMBL:OAH07017.1, ECO:0000313|Proteomes:UP000077333};
RN [1] {ECO:0000313|EMBL:OAH07017.1, ECO:0000313|Proteomes:UP000077333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB2 {ECO:0000313|EMBL:OAH07017.1,
RC ECO:0000313|Proteomes:UP000077333};
RA Poehlein A., Billerbeck S., Voget S., Wemheuer B., Giebel H.-A.,
RA Brinkhoff T., Daniel R., Simon M.;
RT "A new prominent pelagic Roseobacter clade subcluster - CHAB-I-5:
RT biogeography and genomic comparison to other roseobacters.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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:OAH07017.1}.
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DR EMBL; LGRT01000023; OAH07017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177H9T0; -.
DR STRING; 1689867.pfor_22c2553; -.
DR PATRIC; fig|1689867.3.peg.2031; -.
DR OrthoDB; 9796205at2; -.
DR Proteomes; UP000077333; Unassembled WGS sequence.
DR GO; GO:0047449; F:2-dehydro-3-deoxy-L-arabinonate dehydratase activity; IEA:UniProtKB-EC.
DR CDD; cd00408; DHDPS-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR PANTHER; PTHR12128:SF73; 4-HYDROXY-TETRAHYDRODIPICOLINATE SYNTHASE; 1.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000077333}.
FT BINDING 210
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 303 AA; 33093 MW; 40BF76D75AE7D490 CRC64;
MTQYSGIWPV APTPFFEDGA VDFDGMKRVL DCLIDQGADG ICILANFSEQ FLISDAERDA
LARLCVEHIA GRVPIIVTIS HFATQIAVER ARFAKEIGAD IVMMMPPYHG ALLKGNAQQS
FEQFAAVGEV GIPIMVQDAP LSGVELPVPL LLRMAREIEM VKLFKIECPR ASNKLRALIA
EGREAIEAPF DGEEAITLLA DLDAGATGSM TSGMIVDQIK PVITHHLAGR IEEATTAYGR
VAMVINHENR QCGWQSCKAA MVAGGVIKSD YCRHPIEPLH PEIKSRLIDL LKPLDPLVLR
WGV
//
