GAPOR_PYRFU
ID GAPOR_PYRFU Reviewed; 653 AA.
AC Q8U3K2; O93720; Q9UWI2;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Glyceraldehyde-3-phosphate:ferredoxin oxidoreductase {ECO:0000312|EMBL:AAL80588.1};
DE Short=GAPOR {ECO:0000303|PubMed:9774434};
DE EC=1.2.7.6 {ECO:0000269|PubMed:11265456, ECO:0000269|PubMed:7721730};
DE AltName: Full=Tungsten-containing glyceraldehyde-3-phosphate ferredoxin oxidoreductase;
GN Name=gor {ECO:0000312|EMBL:AAC70892.1}; OrderedLocusNames=PF0464;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC70892.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND EPR SPECTROSCOPY.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
RC {ECO:0000312|EMBL:AAC70892.1};
RX PubMed=9774434; DOI=10.1074/jbc.273.43.28149;
RA van der Oost J., Schut G., Kengen S.W., Hagen W.R., Thomm M., de Vos W.M.;
RT "The ferredoxin-dependent conversion of glyceraldehyde-3-phosphate in the
RT hyperthermophilic archaeon Pyrococcus furiosus represents a novel site of
RT glycolytic regulation.";
RL J. Biol. Chem. 273:28149-28154(1998).
RN [2] {ECO:0000312|EMBL:AAL80588.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-38, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 {ECO:0000269|PubMed:7721730};
RX PubMed=7721730; DOI=10.1074/jbc.270.15.8389;
RA Mukund S., Adams M.W.;
RT "Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-
RT containing enzyme with a potential glycolytic role in the hyperthermophilic
RT archaeon Pyrococcus furiosus.";
RL J. Biol. Chem. 270:8389-8392(1995).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
RC {ECO:0000269|PubMed:11265456};
RX PubMed=11265456; DOI=10.1016/s0076-6879(01)31052-2;
RA Roy R., Menon A.L., Adams M.W.;
RT "Aldehyde oxidoreductases from Pyrococcus furiosus.";
RL Methods Enzymol. 331:132-144(2001).
CC -!- FUNCTION: Glycolytic enzyme that acts in the place of glyceraldehyde-3-
CC phosphate dehydrogenase (GAPDH) and phosphoglycerate kinase (PGK).
CC Plays a role in anabolic gluconeogenesis. {ECO:0000269|PubMed:11265456,
CC ECO:0000269|PubMed:7721730, ECO:0000269|PubMed:9774434}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + H2O + 2 oxidized [2Fe-2S]-
CC [ferredoxin] = (2R)-3-phosphoglycerate + 3 H(+) + 2 reduced [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:24148, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:58272, ChEBI:CHEBI:59776; EC=1.2.7.6;
CC Evidence={ECO:0000269|PubMed:11265456, ECO:0000269|PubMed:7721730};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:7721730};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000269|PubMed:7721730};
CC -!- COFACTOR:
CC Name=W-bis(molybdopterin guanine dinucleotide); Xref=ChEBI:CHEBI:60537;
CC Evidence={ECO:0000269|PubMed:7721730};
CC Note=Binds 1 W-bis(molybdopterin guanine dinucleotide) (W-bis-MGD)
CC cofactor per subunit. {ECO:0000269|PubMed:7721730};
CC -!- ACTIVITY REGULATION: Activity increased by 58%-93% in the presence of
CC acetyl phosphate, 3-phosphoglycerate or 2,3-bisphosphoglycerate at 10
CC mM concentration. Inhibited by up to 25% in the presence of
CC crotonaldehyde or formaldehyde at 10 mM concentration. Inhibited by up
CC to 50% by sodium dithionate. 3.5-fold increase in activity observed by
CC addition of potassium phosphate or sodium arsenate at 200 mM
CC concentration. Activity enhanced by potassium chloride, sodium citrate
CC or sodium sulfate at 200 mM concentration. Sensitive to oxygen.
CC {ECO:0000269|PubMed:11265456, ECO:0000269|PubMed:7721730}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for glyceraldehyde-3-phosphate {ECO:0000269|PubMed:11265456,
CC ECO:0000269|PubMed:7721730};
CC KM=0.43 mM for benzyl viologen {ECO:0000269|PubMed:11265456,
CC ECO:0000269|PubMed:7721730};
CC KM=6 uM for ferredoxin (in the presence of 0.40 mM GAP)
CC {ECO:0000269|PubMed:11265456, ECO:0000269|PubMed:7721730};
CC KM=28 uM for glyceraldehyde-3-phosphate (in the presence of 100 uM
CC ferredoxin) {ECO:0000269|PubMed:11265456,
CC ECO:0000269|PubMed:7721730};
CC Vmax=350 umol/min/mg enzyme with glyceraldehyde-3-phosphate as
CC substrate (in the presence of 3 mM benzyl viologen)
CC {ECO:0000269|PubMed:11265456, ECO:0000269|PubMed:7721730};
CC Vmax=310 umol/min/mg enzyme with benzyl viologen as substrate
CC {ECO:0000269|PubMed:11265456, ECO:0000269|PubMed:7721730};
CC Vmax=90 umol/min/mg enzyme with ferredoxin as substrate
CC {ECO:0000269|PubMed:11265456, ECO:0000269|PubMed:7721730};
CC Vmax=78 umol/min/mg enzyme with glyceraldehyde-3-phosphate as
CC substrate (in the presence of 100 uM ferredoxin)
CC {ECO:0000269|PubMed:11265456, ECO:0000269|PubMed:7721730};
CC Temperature dependence:
CC Stable at 80 degrees Celsius for 15 minutes.
CC {ECO:0000269|PubMed:11265456, ECO:0000269|PubMed:7721730};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7721730}.
CC -!- MISCELLANEOUS: Two zinc atoms per subunit with no known function have
CC been observed. {ECO:0000269|PubMed:11265456}.
CC -!- SIMILARITY: Belongs to the AOR/FOR family. {ECO:0000255}.
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DR EMBL; U74298; AAC70892.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL80588.1; -; Genomic_DNA.
DR PIR; A56374; A56374.
DR RefSeq; WP_011011581.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U3K2; -.
DR SMR; Q8U3K2; -.
DR IntAct; Q8U3K2; 1.
DR STRING; 186497.PF0464; -.
DR PRIDE; Q8U3K2; -.
DR EnsemblBacteria; AAL80588; AAL80588; PF0464.
DR GeneID; 41712265; -.
DR KEGG; pfu:PF0464; -.
DR PATRIC; fig|186497.12.peg.488; -.
DR eggNOG; arCOG05072; Archaea.
DR HOGENOM; CLU_440510_0_0_2; -.
DR OMA; CRFHRGW; -.
DR OrthoDB; 5023at2157; -.
DR PhylomeDB; Q8U3K2; -.
DR BRENDA; 1.2.7.6; 5243.
DR SABIO-RK; Q8U3K2; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0043797; F:glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006110; P:regulation of glycolytic process; IDA:UniProtKB.
DR Gene3D; 1.10.569.10; -; 1.
DR Gene3D; 3.60.9.10; -; 1.
DR InterPro; IPR013984; Ald_Fedxn_OxRdtase_dom2.
DR InterPro; IPR013983; Ald_Fedxn_OxRdtase_N.
DR InterPro; IPR036503; Ald_Fedxn_OxRdtase_N_sf.
DR InterPro; IPR001203; OxRdtase_Ald_Fedxn_C.
DR InterPro; IPR036021; Tungsten_al_ferr_oxy-like_C.
DR Pfam; PF01314; AFOR_C; 1.
DR Pfam; PF02730; AFOR_N; 1.
DR SMART; SM00790; AFOR_N; 1.
DR SUPFAM; SSF48310; SSF48310; 1.
DR SUPFAM; SSF56228; SSF56228; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Reference proteome; Tungsten; Zinc.
FT CHAIN 1..653
FT /note="Glyceraldehyde-3-phosphate:ferredoxin
FT oxidoreductase"
FT /id="PRO_0000419806"
FT CONFLICT 493
FT /note="E -> D (in Ref. 1; AAC70892)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="W -> C (in Ref. 1; AAC70892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 653 AA; 73948 MW; 0ADAC8E59E8884AD CRC64;
MKFSVLKLDV GKREVEAQEI EREDIFGVVD YGIMRHNELR TYEVDPYDPR NIVIFGIGPF
AGSVLPGSHR LVFFFRSPLY GGLFPSTMGG AGYQFKNVGV DFVEIHGKAE KPTVIILKND
GEKLSVDFYE IELEKLLDVW KEYKGEEGVY ALTQYLLDNL ASVFEGMEFR IAVVGPAALN
TNMGAIFSQA LRNGKRAVGS EDWAARGGPG SVLLRAHNVV AIAFGGKKRK REFPGEDISD
VKVAKRVVEG IHKKAQRDVI NESTVKYRYN PKLNTGGTFG GNYPAEGDLV PVLNWQMPYI
PKEERIKIHE LIMKYYWEPF NKESIQPKNW TTCGEPCPVV CKKHRKGHHV EYEPYEANGP
LSGSIYLYAS DISVHAVDAM GFDAIEFGGT AAWVLELVHK GLLKPAEVGI SDVPEFTKDD
LITKPVEASE KNAKLVAELA HSIAFGKTEV ARIIGMGKRK ASKILDEKFK DRLSYGESFK
DYGVYTPLGD DGEINPTMYW AIGNFIPLPI QGRYWTFYQF GVFLEPEELA QKIVSSALWE
FWYDNVGWCR FHRGWMKKVL KALFMEAYGV SIDMEEHAKK QIRKLIDYLK KAGYEPVFWD
SMRVIDLVAK GSEEFGNENW AKKFKEDKIG TAKEYLKRVL DAYSQLIGTE WTL
