KGSDH_SACS2
ID KGSDH_SACS2 Reviewed; 478 AA.
AC Q97UA1;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=2,5-dioxopentanoate dehydrogenase;
DE EC=1.2.1.26;
DE AltName: Full=Aldehyde dehydrogenase T;
DE AltName: Full=Alpha-ketoglutaric semialdehyde dehydrogenase AldhT;
GN Name=aldhT; OrderedLocusNames=SSO3117;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP INDUCTION.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
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).
CC -!- FUNCTION: 2,5-dioxopentanoate dehydrogenase involved in the degradation
CC of pentoses such as D-arabinose or D-xylose, a major component of
CC hemicelluloses such as xylan. Catalyzes the fifth reaction in the
CC pentose utilization pathway through dehydratation of 2,5-
CC dioxopentanoate into 2-oxoglutarate. Shows also dehydrogenase activity
CC toward glycolaldehyde and DL-glyceraldehyde.
CC {ECO:0000269|PubMed:16849334}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,5-dioxopentanoate + H2O + NADP(+) = 2-oxoglutarate + 2 H(+)
CC + NADPH; Xref=Rhea:RHEA:11296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58136,
CC ChEBI:CHEBI:58349; EC=1.2.1.26;
CC Evidence={ECO:0000269|PubMed:16849334};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:16849334};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16849334}.
CC -!- INDUCTION: Expression is highly induced during growth on D-arabinose.
CC The promoter contains the conserved cis-regulatory element 5'-AACATGTT-
CC 3' ARA-box found in arabinose-induced genes.
CC {ECO:0000269|PubMed:16849334}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AE006641; AAK43220.1; -; Genomic_DNA.
DR PIR; E90495; E90495.
DR RefSeq; WP_009990943.1; NC_002754.1.
DR AlphaFoldDB; Q97UA1; -.
DR SMR; Q97UA1; -.
DR STRING; 273057.SSO3117; -.
DR EnsemblBacteria; AAK43220; AAK43220; SSO3117.
DR GeneID; 44128838; -.
DR KEGG; sso:SSO3117; -.
DR PATRIC; fig|273057.12.peg.3225; -.
DR eggNOG; arCOG01252; Archaea.
DR HOGENOM; CLU_005391_0_1_2; -.
DR InParanoid; Q97UA1; -.
DR OMA; PMPIAAW; -.
DR PhylomeDB; Q97UA1; -.
DR BioCyc; MetaCyc:MON-13207; -.
DR BRENDA; 1.2.1.22; 6163.
DR BRENDA; 1.2.1.26; 6163.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0047533; F:2,5-dioxovalerate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0019568; P:arabinose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Arabinose catabolism; Carbohydrate metabolism; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..478
FT /note="2,5-dioxopentanoate dehydrogenase"
FT /id="PRO_0000428928"
FT ACT_SITE 249
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 283
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 148..149
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 172..175
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 225..226
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 478 AA; 52290 MW; 48D83AADC1B0686C CRC64;
MKSYQGLADK WIKGSGEEYL DINPADKDHV LAKIRLYTKD DVKEAINKAV AKFDEWSRTP
APKRGSILLK AGELMEQEAQ EFALLMTLEE GKTLKDSMFE VTRSYNLLKF YGALAFKISG
KTLPSADPNT RIFTVKEPLG VVALITPWNF PLSIPVWKLA PALAAGNTAV IKPATKTPLM
VAKLVEVLSK AGLPEGVVNL VVGKGSEVGD TIVSDDNIAA VSFTGSTEVG KRIYKLVGNK
NRMTRIQLEL GGKNALYVDK SADLTLAAEL AVRGGFGLTG QSCTATSRLI INKDVYTQFK
QRLLERVKKW RVGPGTEDVD MGPVVDEGQF KKDLEYIEYG KNVGAKLIYG GNIIPGKGYF
LEPTIFEGVT SDMRLFKEEI FGPVLSVTEA KDLDEAIRLV NAVDYGHTAG IVASDIKAIN
EFVSRVEAGV IKVNKPTVGL ELQAPFGGFK NSGATTWKEM GEDALEFYLK EKTVYEGW
