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NAD-specific glutamate dehydrogenase A (NAD-GDH A) (EC 1.4.1.2)

 DHE2_HALSI              Reviewed;         435 AA.
P29051;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 1.
05-DEC-2018, entry version 86.
RecName: Full=NAD-specific glutamate dehydrogenase A;
Short=NAD-GDH A;
EC=1.4.1.2;
Name=gdhX; Synonyms=gdhA;
Halobacterium salinarum (Halobacterium halobium).
Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
Halobacteriales; Halobacteriaceae; Halobacterium.
NCBI_TaxID=2242;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CCM 2090 / JCM 9120;
PubMed=1766432; DOI=10.1007/BF00280290;
Benachenhou N., Baldacci G.;
"The gene for a halophilic glutamate dehydrogenase: sequence,
transcription analysis and phylogenetic implications.";
Mol. Gen. Genet. 230:345-352(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=NRC-36014;
PubMed=15780999; DOI=10.1016/j.gene.2005.01.011;
Ingoldsby L.M., Geoghegan K.F., Hayden B.M., Engel P.C.;
"The discovery of four distinct glutamate dehydrogenase genes in a
strain of Halobacterium salinarum.";
Gene 349:237-244(2005).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 119-128;
184-193 AND 268-276, CHARACTERIZATION, AND CATALYTIC ACTIVITY.
STRAIN=NRC-36014;
PubMed=12052548; DOI=10.1111/j.1574-6968.2002.tb11200.x;
Hayden B.M., Bonete M.J., Brown P.E., Moir A.J., Engel P.C.;
"Glutamate dehydrogenase of Halobacterium salinarum: evidence that the
gene sequence currently assigned to the NADP+-dependent enzyme is in
fact that of the NAD+-dependent glutamate dehydrogenase.";
FEMS Microbiol. Lett. 211:37-41(2002).
[4]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
REGULATION.
STRAIN=NRC-36014;
PubMed=22527040; DOI=10.1007/s00792-012-0446-z;
Munawar N., Engel P.C.;
"Overexpression in a non-native halophilic host and biotechnological
potential of NAD+-dependent glutamate dehydrogenase from Halobacterium
salinarum strain NRC-36014.";
Extremophiles 16:463-476(2012).
-!- CATALYTIC ACTIVITY:
Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH
+ NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938,
ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
EC=1.4.1.2; Evidence={ECO:0000269|PubMed:12052548,
ECO:0000269|PubMed:22527040};
-!- ACTIVITY REGULATION: Inhibited by ethanol, acetone, acetonitrile
and 2-propanol (65 to 70% inhibition) and to a lesser extent by
methanol and dimethyl formamide (26 and 49 % inhibition
respectively). No effect of glycerol or DMSO.
{ECO:0000269|PubMed:22527040}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=14 mM for glutamate (for the recombinant enzyme, in the
presence of 3.2 M NaCl) {ECO:0000269|PubMed:22527040};
KM=0.35 mM for NAD(+) (for the recombinant enzyme, in the
presence of 3.2 M NaCl) {ECO:0000269|PubMed:22527040};
KM=3.4 mM for 2-oxoglutarate (for the recombinant enzyme, in the
presence of 3.2 M NaCl) {ECO:0000269|PubMed:22527040};
KM=118 mM for NH(4)(+) (for the recombinant enzyme, in the
presence of 3.2 M NaCl) {ECO:0000269|PubMed:22527040};
KM=0.011 mM for NADH (for the recombinant enzyme, in the
presence of 3.2 M NaCl) {ECO:0000269|PubMed:22527040};
KM=9 mM for glutamate (for the recombinant enzyme, in the
presence of 10% DMSO) {ECO:0000269|PubMed:22527040};
KM=0.13 mM for NAD(+) (for the recombinant enzyme, in the
presence of 10% DMSO) {ECO:0000269|PubMed:22527040};
KM=0.8 mM for 2-oxoglutarate (for the recombinant enzyme, in the
presence of 20% DMSO) {ECO:0000269|PubMed:22527040};
KM=112 mM for NH(4)(+) (for the recombinant enzyme, in the
presence of 20% DMSO) {ECO:0000269|PubMed:22527040};
KM=0.025 mM for NADH (for the recombinant enzyme, in the
presence of 20% DMSO) {ECO:0000269|PubMed:22527040};
Note=kcat is 24 sec(-1) for glutamate in the presence of 3.2 M
NaCl. kcat is 16 sec(-1) for NAD(+) in the presence of 3.2 M
NaCl. kcat is 56 sec(-1) for 2-oxoglutarate in the presence of
3.2 M NaCl. kcat is 85 sec(-1) for NH(4)(+) in the presence of
3.2 M NaCl. kcat is 39 sec(-1) for NADH in the presence of 3.2 M
NaCl. kcat is 17 sec(-1) for glutamate in the presence of 10%
DMSO. kcat is 15 sec(-1) for NAD(+) in the presence of 10% DMSO.
kcat is 46 sec(-1) for 2-oxoglutarate in the presence of 20%
DMSO. kcat is 84 sec(-1) for NH(4)(+) in the presence of 20%
DMSO. kcat is 47 sec(-1) for NADH in the presence of 20% DMSO.;
pH dependence:
Optimum pH for oxidative deamination is 9.2. Optimum pH for
reductive amination is 8.5. {ECO:0000269|PubMed:22527040};
Temperature dependence:
Optimum temperature is 70 degrees Celsius. The enzyme is
entirely stable from 50 to 70 degrees Celsius and 55 % activity
is retained after 30 min at 90 degrees Celsius.
{ECO:0000269|PubMed:22527040};
-!- SUBUNIT: Homohexamer. {ECO:0000250}.
-!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:12052548}.
-!- MISCELLANEOUS: Strain NRC-36014 contains 4 distinct glutamate
dehydrogenases while strain NRC-1 contains only 3. GdhX is only
present in strain NRC-36014 (PubMed:15780999).
{ECO:0000305|PubMed:15780999}.
-!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
{ECO:0000305}.
-!- CAUTION: Was initially thought to be a NADP-specific glutamate
dehydrogenase. {ECO:0000305|PubMed:1766432}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X63837; CAA45327.1; -; Genomic_DNA.
EMBL; AY840088; AAW19068.1; -; Genomic_DNA.
PIR; S18609; S18609.
ProteinModelPortal; P29051; -.
SMR; P29051; -.
BioCyc; MetaCyc:MONOMER-741; -.
BRENDA; 1.4.1.2; 2552.
GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
CDD; cd01076; NAD_bind_1_Glu_DH; 1.
InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
InterPro; IPR014362; Glu_DH.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR033922; NAD_bind_Glu_DH.
Pfam; PF00208; ELFV_dehydrog; 1.
Pfam; PF02812; ELFV_dehydrog_N; 1.
PIRSF; PIRSF000185; Glu_DH; 1.
PRINTS; PR00082; GLFDHDRGNASE.
SMART; SM00839; ELFV_dehydrog; 1.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
1: Evidence at protein level;
Direct protein sequencing; NAD; Oxidoreductase.
CHAIN 1 435 NAD-specific glutamate dehydrogenase A.
/FTId=PRO_0000182779.
ACT_SITE 126 126 {ECO:0000255|PROSITE-ProRule:PRU10011}.
SEQUENCE 435 AA; 47459 MW; 0E4E940D2FF8B9D2 CRC64;
MTMASKSDST HDESGDEAAD STEPESALET ARRQLYHAAS YLDIDQNIVE RLKYPKKVHE
VTIPIERDDG TVEVFTGYRA QHDSVRGPYK GGLRYHPDVT RDECVGLGMW MTWKCAVMDL
PFGGAKGGVA VNPKELSPEE KERLTRRFTQ EIRDVIGPNQ DIPAPDMGTD PQTMAWLMDA
YSMQEGETTP GVVTGKPPVV GGSEGREEAP GRSVAIITQL VCEYYDQPLD ETTVAVQGYG
SVGANAARLL DKWGATIVAI SDVNGAMYEP DGIDTASVPS HDEEPEAVTT YADTVISNEE
LLTLDVDVLI PAALGNVITK ENAEAIAADL VVEGANGPTT STADSILADR DVAVIPDILA
NAGGVTVSYF EWLQDINRRA WSLERVNDEL EAEMQAAWRA VKDEYENRDV TWRDAAYIVA
LSRIAEAHEA RGLWP


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Pathways :
WP1051: GPCRs, Class C Metabotropic glutamate, pheromone
WP1167: GPCRs, Class C Metabotropic glutamate, pheromone
WP1373: GPCRs, Class C Metabotropic glutamate, pheromone
WP1493: Carbon assimilation C4 pathway
WP1566: Citrate cycle (TCA cycle)
WP1567: Glycolysis and Gluconeogenesis
WP1581: Histidine metabolism
WP1612: 1,2-Dichloroethane degradation
WP1614: 1- and 2-Methylnaphthalene degradation
WP1615: 3-Chloroacrylic acid degradation
WP1617: Alanine, aspartate and glutamate metabolism
WP1621: Arginine and proline metabolism
WP1622: Ascorbate and aldarate metabolism
WP1626: Benzoate degradation via CoA ligation
WP1627: Benzoate degradation via hydroxylation
WP1628: beta-Alanine metabolism
WP1633: Bisphenol A degradation
WP1634: Butanoate metabolism
WP1643: D-Glutamine and D-glutamate metabolism
WP1647: Fatty acid biosynthesis
WP1652: Fructose and mannose metabolism
WP1654: gamma-Hexachlorocyclohexane degradation
WP1655: Geraniol degradation
WP1657: Glycerolipid metabolism
WP1665: Limonene and pinene degradation

Related Genes :
[rocG gudA yweB BSU37790 ipa-75d] Catabolic NAD-specific glutamate dehydrogenase RocG (NAD-GDH) (EC 1.4.1.2) (Glutamate dehydrogenase) (GlutDH) (Trigger enzyme RocG)
[gdh] NAD-specific glutamate dehydrogenase (NAD-GDH) (EC 1.4.1.2)
[gdh] Glucose 1-dehydrogenase (GDH) (GlcDH) (EC 1.1.1.47) (Aldose 1-dehydrogenase [NAD(P)(+)]) (EC 1.1.1.359) (Galactose 1-dehydrogenase) (EC 1.1.1.120) (EC 1.1.1.48)
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[gdhX gdhA] NAD-specific glutamate dehydrogenase A (NAD-GDH A) (EC 1.4.1.2)
[iolA mmsA yxdA BSU39760 E83A] Malonate-semialdehyde dehydrogenase (MSA dehydrogenase) (EC 1.2.1.-) (Methylmalonate-semialdehyde dehydrogenase) (MMSA dehydrogenase) (MMSDH) (MSDH) (EC 1.2.1.27)
[GLUD1 GLUD] Glutamate dehydrogenase 1, mitochondrial (GDH 1) (EC 1.4.1.3)
[gdh MSMEG_4699 MSMEI_4582] NAD-specific glutamate dehydrogenase (NAD-GDH) (EC 1.4.1.2) (NAD(+)-dependent glutamate dehydrogenase)
[gdhA b1761 JW1750] NADP-specific glutamate dehydrogenase (NADP-GDH) (EC 1.4.1.4)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[putA STM1124] Bifunctional protein PutA [Includes: Proline dehydrogenase (EC 1.5.5.2) (Proline oxidase); Delta-1-pyrroline-5-carboxylate dehydrogenase (P5C dehydrogenase) (EC 1.2.1.88) (L-glutamate gamma-semialdehyde dehydrogenase)]
[ALDH4A1 ALDH4 P5CDH] Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (P5C dehydrogenase) (EC 1.2.1.88) (Aldehyde dehydrogenase family 4 member A1) (L-glutamate gamma-semialdehyde dehydrogenase)
[IDH3A] Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial (EC 1.1.1.41) (Isocitric dehydrogenase subunit alpha) (NAD(+)-specific ICDH subunit alpha)
[Aldh3a1 Ahd-4 Ahd4 Aldh3 Aldh4] Aldehyde dehydrogenase, dimeric NADP-preferring (EC 1.2.1.5) (Aldehyde dehydrogenase 4) (Aldehyde dehydrogenase family 3 member A1) (Dioxin-inducible aldehyde dehydrogenase 3)
[ard-1 NCU00643] L-arabinitol 4-dehydrogenase (LAD) (EC 1.1.1.12)
[IDH2 YOR136W O3326 YOR3326W] Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial (EC 1.1.1.41) (Isocitric dehydrogenase) (NAD(+)-specific ICDH)
[nnrD nnrE DU31_11450 DU33_17155 DU34_07685 DU35_07085 DU36_09790 DU37_12565 DU38_10935 DU39_12815 DU40_12880 DU41_14740 DU42_07270 DU44_01295 DU45_16155 DU46_10990 DU47_01255 DU48_07720 DU49_14655 DU50_12285 DU51_19805 DU54_00670 DU55_05370 DU56_15760 DU57_06830 DU59_03855 DU60_14595 DU61_11015 DU62_06475 DU63_06395 DU64_18510 DU65_03810 DU66_17325 DU68_15815 DU69_04530 DU71_00795 DU72_19440 DU73_09980 DU74_18275 DU75_11940 DU76_10140 DU77_00515 DU78_12025 DU79_00590 DU80_09755 DU81_02350 DU82_01250 DU83_01980 DU84_01080 DU85_13135 DU86_12110 DU88_12415] Multifunctional fusion protein [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6) (NAD(P)HX epimerase)]
[Aldh4a1] Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (P5C dehydrogenase) (EC 1.2.1.88) (Aldehyde dehydrogenase family 4 member A1) (L-glutamate gamma-semialdehyde dehydrogenase)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); 3C-like serine proteinase (3CLSP) (EC 3.4.21.-) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); 3C-like serine proteinase (3CLSP) (EC 3.4.21.-) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[gdh am 18F11.230 NCU01195] NADP-specific glutamate dehydrogenase (NADP-GDH) (EC 1.4.1.4) (NADP-dependent glutamate dehydrogenase)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[IDH1 YNL037C N2690] Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial (EC 1.1.1.41) (Isocitric dehydrogenase) (NAD(+)-specific ICDH)

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