G6PD_HALVD
ID G6PD_HALVD Reviewed; 262 AA.
AC D4GS48;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=NAD-dependent glucose-6-phosphate dehydrogenase {ECO:0000305};
DE Short=Glc6PDH {ECO:0000303|PubMed:25836736};
DE EC=1.1.1.388 {ECO:0000269|PubMed:25836736};
DE AltName: Full=Archaeal zwischenferment {ECO:0000303|PubMed:25836736};
GN Name=azf {ECO:0000303|PubMed:25836736};
GN OrderedLocusNames=HVO_0511 {ECO:0000312|EMBL:ADE03728.1};
GN ORFNames=C498_16134 {ECO:0000312|EMBL:ELY25894.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=H26;
RX PubMed=25836736; DOI=10.1016/j.febslet.2015.03.026;
RA Pickl A., Schoenheit P.;
RT "The oxidative pentose phosphate pathway in the haloarchaeon Haloferax
RT volcanii involves a novel type of glucose-6-phosphate dehydrogenase -- The
RT archaeal Zwischenferment.";
RL FEBS Lett. 589:1105-1111(2015).
CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation of glucose 6-phosphate
CC to 6-phosphogluconolactone. {ECO:0000269|PubMed:25836736}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NAD(+) = 6-phospho-D-glucono-1,5-
CC lactone + H(+) + NADH; Xref=Rhea:RHEA:38215, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57955,
CC ChEBI:CHEBI:61548; EC=1.1.1.388;
CC Evidence={ECO:0000269|PubMed:25836736};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 mM for glucose 6-phosphate {ECO:0000269|PubMed:25836736};
CC KM=0.43 mM for NAD(+) {ECO:0000269|PubMed:25836736};
CC KM=5.2 mM for NADP(+) {ECO:0000269|PubMed:25836736};
CC Vmax=212 umol/min/mg enzyme (with NAD(+) as electron acceptor)
CC {ECO:0000269|PubMed:25836736};
CC Vmax=11 umol/min/mg enzyme (with NADP(+) as electron acceptor)
CC {ECO:0000269|PubMed:25836736};
CC Note=The catalytic efficiency with NAD(+) is about 230-fold higher
CC than with NADP(+), indicating that NAD(+) is the physiological
CC electron acceptor. {ECO:0000269|PubMed:25836736};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:25836736};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC {ECO:0000269|PubMed:25836736}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25836736}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants do not grow on glucose.
CC {ECO:0000269|PubMed:25836736}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; CP001956; ADE03728.1; -; Genomic_DNA.
DR EMBL; AOHU01000100; ELY25894.1; -; Genomic_DNA.
DR RefSeq; WP_004044412.1; NZ_AOHU01000100.1.
DR AlphaFoldDB; D4GS48; -.
DR SMR; D4GS48; -.
DR STRING; 309800.C498_16134; -.
DR EnsemblBacteria; ADE03728; ADE03728; HVO_0511.
DR EnsemblBacteria; ELY25894; ELY25894; C498_16134.
DR GeneID; 8925817; -.
DR KEGG; hvo:HVO_0511; -.
DR PATRIC; fig|309800.29.peg.3125; -.
DR eggNOG; arCOG04704; Archaea.
DR HOGENOM; CLU_079334_1_0_2; -.
DR OMA; RYYFDRF; -.
DR OrthoDB; 43299at2157; -.
DR BioCyc; MetaCyc:MON-20543; -.
DR BRENDA; 1.1.1.388; 2561.
DR UniPathway; UPA00115; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_02046; Glc6PDH_archaea; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR032884; Glc6PDH_archaea.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glucose metabolism; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..262
FT /note="NAD-dependent glucose-6-phosphate dehydrogenase"
FT /id="PRO_0000434433"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P09147, ECO:0000255|HAMAP-
FT Rule:MF_02046"
FT BINDING 90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P09147, ECO:0000255|HAMAP-
FT Rule:MF_02046"
FT BINDING 115
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P09147, ECO:0000255|HAMAP-
FT Rule:MF_02046"
FT BINDING 152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P09147, ECO:0000255|HAMAP-
FT Rule:MF_02046"
FT BINDING 156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P09147, ECO:0000255|HAMAP-
FT Rule:MF_02046"
SQ SEQUENCE 262 AA; 29365 MW; 0B789A0FA2D6015B CRC64;
MDQPVLLTGA GGRVGQAILG HIGDAYDWRL LDREPLSDEK IPDSVDSTEV YVADVTDETA
VRNAMDGVHA VIHLAGDPRP EAPWDSVLRN NIDGTQQMFD AAVDVGVEKF AFASSNHAVG
AYETTDRTPD MYRPHHEFRL DGTELPRPSN LYGVSKAAGE TLGRYYHDHH DISVVNVRIG
NLTQHHPPKE YERGQAMWLS YRDCGHLFEC CIEADYDYEI VYGISDNDRK YYSIDRARAV
LGYDPQDNSA EFTFEGEPLD EA
