KGSDH_HALVD
ID KGSDH_HALVD Reviewed; 482 AA.
AC D4GP41;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Alpha-ketoglutarate semialdehyde dehydrogenase {ECO:0000303|PubMed:19584053};
DE Short=KGSADH {ECO:0000303|PubMed:19584053};
DE EC=1.2.1.26 {ECO:0000269|PubMed:19584053};
GN Name=xacF {ECO:0000303|PubMed:25141768}; OrderedLocusNames=HVO_B0039;
GN ORFNames=C498_01560;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OG Plasmid pHV3.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP PROTEIN SEQUENCE OF 1-19, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=DS2 / DS70;
RX PubMed=19584053; DOI=10.1074/jbc.m109.003814;
RA Johnsen U., Dambeck M., Zaiss H., Fuhrer T., Soppa J., Sauer U.,
RA Schonheit P.;
RT "D-xylose degradation pathway in the halophilic archaeon Haloferax
RT volcanii.";
RL J. Biol. Chem. 284:27290-27303(2009).
RN [4]
RP INDUCTION.
RX PubMed=25141768; DOI=10.1111/1462-2920.12603;
RA Johnsen U., Sutter J.M., Schulz A.C., Taestensen J.B., Schoenheit P.;
RT "XacR - a novel transcriptional regulator of D-xylose and L-arabinose
RT catabolism in the haloarchaeon Haloferax volcanii.";
RL Environ. Microbiol. 17:1663-1676(2015).
CC -!- FUNCTION: Alpha-ketoglutarate semialdehyde dehydrogenase involved in
CC the degradation of D-xylose, a major component of hemicelluloses such
CC as xylan. Catalyzes the fifth reaction in the xylose utilization
CC pathway through dehydratation of alpha-ketoglutarate semialdehyde (2,5-
CC dioxopentanoate) into alpha-ketoglutarate.
CC {ECO:0000269|PubMed:19584053}.
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:19584053};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.03 mM for NADP(+) {ECO:0000269|PubMed:19584053};
CC KM=2.6 mM for NAD(+) {ECO:0000269|PubMed:19584053};
CC KM=1.16 mM for glutaraldehyde {ECO:0000269|PubMed:19584053};
CC KM=6.2 mM for succinate semialdehyde {ECO:0000269|PubMed:19584053};
CC -!- PATHWAY: Carbohydrate metabolism; D-xylose degradation.
CC {ECO:0000269|PubMed:19584053}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19584053}.
CC -!- INDUCTION: Transcriptionally up-regulated by both L-arabinose and D-
CC xylose via the pentose-specific regulator XacR (PubMed:25141768,
CC PubMed:19584053). Expression is repressed by glucose (PubMed:19584053).
CC {ECO:0000269|PubMed:19584053, ECO:0000269|PubMed:25141768}.
CC -!- DISRUPTION PHENOTYPE: Impairs growth on D-xylose as sole energy and
CC carbon substrate. {ECO:0000269|PubMed:19584053}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CP001953; ADE01373.1; -; Genomic_DNA.
DR EMBL; AOHU01000021; ELY36792.1; -; Genomic_DNA.
DR RefSeq; WP_004041115.1; NZ_AOHU01000021.1.
DR AlphaFoldDB; D4GP41; -.
DR SMR; D4GP41; -.
DR STRING; 309800.C498_01560; -.
DR EnsemblBacteria; ADE01373; ADE01373; HVO_B0039.
DR EnsemblBacteria; ELY36792; ELY36792; C498_01560.
DR GeneID; 8919187; -.
DR KEGG; hvo:HVO_B0039; -.
DR PATRIC; fig|309800.29.peg.297; -.
DR eggNOG; arCOG01252; Archaea.
DR HOGENOM; CLU_005391_1_0_2; -.
DR OMA; PMPIAAW; -.
DR OrthoDB; 56373at2157; -.
DR BioCyc; MetaCyc:MON-16377; -.
DR SABIO-RK; D4GP41; -.
DR UniPathway; UPA00810; -.
DR Proteomes; UP000008243; Plasmid pHV3.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0047533; F:2,5-dioxovalerate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0042843; P:D-xylose catabolic process; IEA:UniProtKB-UniPathway.
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; 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.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; NADP; Oxidoreductase;
KW Plasmid; Reference proteome.
FT CHAIN 1..482
FT /note="Alpha-ketoglutarate semialdehyde dehydrogenase"
FT /id="PRO_0000428799"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
SQ SEQUENCE 482 AA; 50657 MW; C3291827DECEFB70 CRC64;
MTDPSKNYVN GEWVTSETGE TTEVTNPANP SEVVAAYQHS NENDAAAAVD AAVAAEDEWR
NTPGPERGRI LREAGTLLAQ RKDELTEILT AEEGKARPEA AGEVQRAIDI FHYFSSKAAD
LGGTKKGASG PNTNLYTRQE PVGVAALITP WNYPIAIPAW KLAPALAAGN TVVLKPASIA
PGVVIEIARA LDEAGLPDGV LNVVTGPGSS VGSEFIGNEG TDLVSFTGSS QVGEMVYEQA
TDAGKRVQTE LGGKNPTLVA DSANPAEAAD IVANGGFGTT GQSCTACSRA IVHEDVYDDF
VAELVDRAES LDVGPGTDHE MGPQVSESEL SSTLEYIDIA EAEGATLVAG GGVPEGEAVE
TGHFVEPTVF TDVDPDMRIA QEEVFGPVVA VIEVSDFDEG LAVANDVDYG LSASIVTDDH
TEANRFVDEV EAGVVKVNDK TTGLELHVPF GGFKRSSSET WREQGDAGLD FYTIEKTVYD
SY
