KDAD_SACS2
ID KDAD_SACS2 Reviewed; 298 AA.
AC Q97UA0;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=2-dehydro-3-deoxy-D-arabinonate dehydratase;
DE EC=4.2.1.141 {ECO:0000305|PubMed:16849334};
DE AltName: Full=2-keto-3-deoxy-D-arabinonate dehydratase {ECO:0000303|PubMed:18448118};
DE Short=KdaD {ECO:0000303|PubMed:16849334};
GN Name=kdaD {ECO:0000303|PubMed:16849334};
GN OrderedLocusNames=SSO3118 {ECO:0000312|EMBL:AAK43221.1};
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057 {ECO:0000312|EMBL:AAK43221.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2
RC {ECO:0000312|Proteomes:UP000001974};
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, SUBUNIT, INDUCTION BY D-ARABINOSE, AND CATALYTIC ACTIVITY.
RX PubMed=16849334; DOI=10.1074/jbc.m605549200;
RA Brouns S.J., Walther J., Snijders A.P., van de Werken H.J., Willemen H.L.,
RA Worm P., de Vos M.G., Andersson A., Lundgren M., Mazon H.F.,
RA van den Heuvel R.H., Nilsson P., Salmon L., de Vos W.M., Wright P.C.,
RA Bernander R., van der Oost J.;
RT "Identification of the missing links in prokaryotic pentose oxidation
RT pathways: evidence for enzyme recruitment.";
RL J. Biol. Chem. 281:27378-27388(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 6-298 IN COMPLEX WITH THE
RP SUBSTRATE ANALOG 2-OXOBUTANOATE; THE PRODUCT 2,5-DIOXOPENTANOATE; CALCIUM
RP AND MAGNESIUM, COFACTOR, AND SUBUNIT.
RX PubMed=18448118; DOI=10.1016/j.jmb.2008.03.064;
RA Brouns S.J., Barends T.R., Worm P., Akerboom J., Turnbull A.P., Salmon L.,
RA van der Oost J.;
RT "Structural insight into substrate binding and catalysis of a novel 2-keto-
RT 3-deoxy-D-arabinonate dehydratase illustrates common mechanistic features
RT of the FAH superfamily.";
RL J. Mol. Biol. 379:357-371(2008).
CC -!- FUNCTION: Participates in a pentose oxidation pathway that converts D-
CC arabinonate to 2-oxoglutarate. {ECO:0000269|PubMed:16849334}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-D-arabinonate = 2,5-dioxopentanoate + H2O;
CC Xref=Rhea:RHEA:35807, ChEBI:CHEBI:15377, ChEBI:CHEBI:16699,
CC ChEBI:CHEBI:58136; EC=4.2.1.141;
CC Evidence={ECO:0000305|PubMed:16849334};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:18448118};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000305|PubMed:18448118};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16849334,
CC ECO:0000269|PubMed:18448118}.
CC -!- INDUCTION: Expression is strongly increased by growth on D-arabinose,
CC both at the mRNA and at the protein level.
CC {ECO:0000269|PubMed:16849334}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR EMBL; AE006641; AAK43221.1; -; Genomic_DNA.
DR PIR; F90495; F90495.
DR PDB; 2Q18; X-ray; 2.10 A; X=6-298.
DR PDB; 2Q19; X-ray; 3.00 A; X=6-298.
DR PDB; 2Q1A; X-ray; 2.50 A; X=6-298.
DR PDB; 2Q1C; X-ray; 2.80 A; X=6-298.
DR PDB; 2Q1D; X-ray; 2.70 A; X=6-298.
DR PDB; 3BQB; X-ray; 2.70 A; A/X/Y/Z=6-298.
DR PDBsum; 2Q18; -.
DR PDBsum; 2Q19; -.
DR PDBsum; 2Q1A; -.
DR PDBsum; 2Q1C; -.
DR PDBsum; 2Q1D; -.
DR PDBsum; 3BQB; -.
DR AlphaFoldDB; Q97UA0; -.
DR SMR; Q97UA0; -.
DR STRING; 273057.SSO3118; -.
DR EnsemblBacteria; AAK43221; AAK43221; SSO3118.
DR KEGG; sso:SSO3118; -.
DR PATRIC; fig|273057.12.peg.3226; -.
DR eggNOG; arCOG00236; Archaea.
DR HOGENOM; CLU_078481_0_0_2; -.
DR InParanoid; Q97UA0; -.
DR OMA; WQIPEPE; -.
DR PhylomeDB; Q97UA0; -.
DR BioCyc; MetaCyc:MON-13206; -.
DR BRENDA; 4.2.1.141; 6163.
DR EvolutionaryTrace; Q97UA0; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0019571; P:D-arabinose catabolic process; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR Gene3D; 3.90.850.10; -; 1.
DR InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR Pfam; PF01557; FAA_hydrolase; 1.
DR SUPFAM; SSF56529; SSF56529; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Lyase; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..298
FT /note="2-dehydro-3-deoxy-D-arabinonate dehydratase"
FT /id="PRO_0000430861"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18448118"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18448118"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18448118"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18448118"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18448118"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18448118"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:2Q18"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2Q1A"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:2Q18"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:2Q18"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:2Q18"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:2Q1A"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:2Q18"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:2Q18"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:2Q18"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:2Q18"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:2Q18"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 222..230
FT /evidence="ECO:0007829|PDB:2Q18"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:2Q18"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:2Q18"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:2Q18"
FT STRAND 285..293
FT /evidence="ECO:0007829|PDB:2Q18"
SQ SEQUENCE 298 AA; 33803 MW; 2FF2C97EDE500AF9 CRC64;
MHFIMMKLFR VVKRGYYISY AILDNSTIIR LDEDPIKALM RYSENKEVLG DRVTGIDYQS
LLKSFQINDI RITKPIDPPE VWGSGISYEM ARERYSEENV AKILGKTIYE KVYDAVRPEI
FFKATPNRCV GHGEAIAVRS DSEWTLPEPE LAVVLDSNGK ILGYTIMDDV SARDLEAENP
LYLPQSKIYA GCCAFGPVIV TSDEIKNPYS LDITLKIVRE GRVFFEGSVN TNKMRRKIEE
QIQYLIRDNP IPDGTILTTG TAIVPGRDKG LKDEDIVEIT ISNIGTLITP VKKRRKIT
