KDADA_AZOBR
ID KDADA_AZOBR Reviewed; 309 AA.
AC Q1JUQ0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=L-2-keto-3-deoxyarabonate dehydratase;
DE Short=L-KDA dehydratase;
DE EC=4.2.1.43;
DE AltName: Full=2-dehydro-3-deoxy-L-arabinonate dehydratase;
DE AltName: Full=L-2-keto-3-deoxyarabinonate dehydratase;
GN Name=araD;
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, FUNCTION,
RP CATALYTIC ACTIVITY, SUBUNIT, PATHWAY, AND MUTAGENESIS OF GLN-143.
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=16950779; DOI=10.1074/jbc.m606727200;
RA Watanabe S., Shimada N., Tajima K., Kodaki T., Makino K.;
RT "Identification and characterization of L-arabonate dehydratase, L-2-keto-
RT 3-deoxyarabonate dehydratase and L-arabinolactonase involved in an
RT alternative pathway of L-arabinose metabolism: novel evolutionary insight
RT into sugar metabolism.";
RL J. Biol. Chem. 281:33521-33536(2006).
RN [2]
RP PATHWAY.
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=6798025; DOI=10.1128/jb.149.1.364-367.1982;
RA Novick N.J., Tyler M.E.;
RT "L-arabinose metabolism in Azospirillum brasiliense.";
RL J. Bacteriol. 149:364-367(1982).
RN [3]
RP CRYSTALLIZATION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=17565178; DOI=10.1107/s1744309107015102;
RA Shimada N., Mikami B., Watanabe S., Makino K.;
RT "Preliminary crystallographic analysis of L-2-keto-3-deoxyarabonate
RT dehydratase, an enzyme involved in an alternative bacterial pathway of L-
RT arabinose metabolism.";
RL Acta Crystallogr. F 63:393-395(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
RA Shimada N., Mikami B., Watanabe S., Kodaki T., Makino K.;
RT "Structural analysis of L-2-keto-3-deoxyarabonate dehydratase an enzyme
RT involved in an alternative bacterial pathway of L-arabinose metabolism in
RT complex with pyruvate.";
RL Submitted (DEC-2008) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the dehydration of L-2-keto-3-deoxyarabonate (L-
CC KDA) to alpha-ketoglutaric semialdehyde (alphaKGSA). Is involved in a
CC degradation pathway of L-arabinose that allows A.brasilense to grow on
CC L-arabinose as a sole carbon source. {ECO:0000269|PubMed:16950779}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-L-arabinonate = 2,5-dioxopentanoate + H2O;
CC Xref=Rhea:RHEA:17201, ChEBI:CHEBI:15377, ChEBI:CHEBI:35173,
CC ChEBI:CHEBI:58136; EC=4.2.1.43;
CC Evidence={ECO:0000269|PubMed:16950779, ECO:0000269|PubMed:17565178};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16950779,
CC ECO:0000269|PubMed:17565178, ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB241136; BAE94270.1; -; Genomic_DNA.
DR PDB; 3FKK; X-ray; 2.10 A; A/B=1-309.
DR PDB; 3FKR; X-ray; 1.80 A; A/B=1-309.
DR PDB; 7C0C; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L=2-309.
DR PDB; 7C0D; X-ray; 1.60 A; A/B/C/D/E/F/G/H/I/J/K/L=2-309.
DR PDB; 7C0E; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=2-309.
DR PDBsum; 3FKK; -.
DR PDBsum; 3FKR; -.
DR PDBsum; 7C0C; -.
DR PDBsum; 7C0D; -.
DR PDBsum; 7C0E; -.
DR AlphaFoldDB; Q1JUQ0; -.
DR SMR; Q1JUQ0; -.
DR BRENDA; 4.2.1.43; 611.
DR EvolutionaryTrace; Q1JUQ0; -.
DR GO; GO:0047449; F:2-dehydro-3-deoxy-L-arabinonate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019570; P:L-arabinose catabolic process to 2-oxoglutarate; IDA:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR SMART; SM01130; DHDPS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arabinose catabolism; Carbohydrate metabolism;
KW Direct protein sequencing; Lyase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16950779"
FT CHAIN 2..309
FT /note="L-2-keto-3-deoxyarabonate dehydratase"
FT /id="PRO_0000418507"
FT ACT_SITE 171
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 143
FT /note="Q->N,E,S,T,Y: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16950779"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 28..40
FT /evidence="ECO:0007829|PDB:7C0D"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:7C0D"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:7C0D"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:7C0D"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:7C0D"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:7C0D"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:7C0D"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3FKR"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:7C0D"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 237..256
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 262..269
FT /evidence="ECO:0007829|PDB:7C0D"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 287..300
FT /evidence="ECO:0007829|PDB:7C0D"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:7C0D"
SQ SEQUENCE 309 AA; 33756 MW; D90AF7B4DAECE06F CRC64;
MTSSSTPRHR GIFPVVPTTF ADTGELDLAS QKRAVDFMID AGSDGLCILA NFSEQFAITD
DERDVLTRTI LEHVAGRVPV IVTTSHYSTQ VCAARSLRAQ QLGAAMVMAM PPYHGATFRV
PEAQIFEFYA RVSDAIAIPI MVQDAPASGT ALSAPFLARM AREIEQVAYF KIETPGAANK
LRELIRLGGD AIEGPWDGEE AITLLADLHA GATGAMTGGG FPDGIRPILE AWREGRHDDA
YARYQAWLPL INHENRQSGI LTAKALMREG GVIASERPRH PMPELHPDTR AELLAIARRL
DPLVLRWAH
