B1YD06

PR
Gene name
gap
Protein name
Glyceraldehyde-3-phosphate dehydrogenase
Names
GAPDH, NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase
Species
Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta) (Thermoproteus neutrophilus)
KEGG Pathway
tne:Tneu_0730
EC number
1.2.1.59: With NAD(+) or NADP(+) as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

54-124 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for B1YD06

Entry ID Method Resolution Chain Position Source
AF-B1YD06-F1 Predicted AlphaFoldDB

No variants for B1YD06

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B1YD06

No associated diseases with B1YD06

6 regional properties for B1YD06

Type Name Position InterPro Accession
domain Immunodeficiency lentiviral matrix, N-terminal 2 - 122 IPR000071
domain Retroviral nucleocapsid Gag protein p24, N-terminal 142 - 248 IPR000721
domain Zinc finger, CCHC-type 386 - 402 IPR001878-1
domain Zinc finger, CCHC-type 407 - 423 IPR001878-2
domain Gag protein p6 445 - 482 IPR014817
domain Retroviral nucleocapsid Gag protein p24, C-terminal domain 276 - 342 IPR045345

Functions

Description
EC Number 1.2.1.59 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

5 GO annotations of molecular function

Name Definition
4-hydroxy-tetrahydrodipicolinate reductase Catalysis of the reaction: (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+.
glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Catalysis of the reaction: D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH + H+.
glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity Catalysis of the reaction: phosphate + NADP+ + glyceraldehyde-3-phosphate = NADPH + 3-phospho-D-glyceroyl-phosphate.
NAD binding Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
NADP binding Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.

2 GO annotations of biological process

Name Definition
glycolytic process The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
lysine biosynthetic process via diaminopimelate The chemical reactions and pathways resulting in the formation of lysine, via the intermediate diaminopimelate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MIRVGIVGYG TIGKRIADAV VAQDDMKIAG VLKVSPDYEA KVAVSRGFPV YTLPDRVEKF
70 80 90 100 110 120
KKAGIEPAGT IEDLIKASDV VVDASPEDVG RENKEKYYQR YDKPVIFQGG EEADVAEVSF
130 140 150 160 170 180
NALANYEEAR GKRYVRVVSC NTTGITRVLT SLTLNGVGIK KARIFIARRG ADPKEHKKGP
190 200 210 220 230 240
INDVVPNPAT VPSHHGPDVQ TILRNVDIVT MAVAVPVTIM HMHMAYIELD SAYPKDQVIE
250 260 270 280 290 300
AFAKTPRIFL ADVGAGFQSL AQVIEYARDL GRPRGDFPEV AVFRDSVTTH GNELYLMYGV
310 320 330 340
HQESIVVPEN IDAIRSIFGT LPKWRSIEKT DKSLKLTTEG KRYG