Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q8ZC51

Entry ID Method Resolution Chain Position Source
AF-Q8ZC51-F1 Predicted AlphaFoldDB

No variants for Q8ZC51

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8ZC51

No associated diseases with Q8ZC51

2 regional properties for Q8ZC51

Type Name Position InterPro Accession
domain Ketopantoate reductase, N-terminal domain 3 - 142 IPR013332
domain Ketopantoate reductase, C-terminal domain 168 - 289 IPR013752

Functions

Description
EC Number 1.1.1.169 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.

2 GO annotations of molecular function

Name Definition
2-dehydropantoate 2-reductase activity Catalysis of the reaction: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH.
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.

1 GO annotations of biological process

Name Definition
pantothenate biosynthetic process The chemical reactions and pathways resulting in the formation of pantothenate, the anion of pantothenic acid. It is a B complex vitamin that is a constituent of coenzyme A and is distributed ubiquitously in foods.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKITVLGCGA LGQLWLSMLH QQDHDVQGWL RVPQPFCSVN VIMLNGESFN RNLTTNDPKH
70 80 90 100 110 120
LLQSELLLVC LKAWQVSSAV TALLPKLNPE CKILLLHNGM GTQEELPLNE HVFLHGVTTH
130 140 150 160 170 180
AARRDGNTII HVASGMTHIG PTSSVIIDDN HLADTLHQAL PDVAWHNDIS AACWQKLAVN
190 200 210 220 230 240
CVINPLTGLY NCRNGDVQRY PELIERLCAE VASVMEMEGY HTSTESLLSY VNNVIRSTAD
250 260 270 280 290 300
NTSSLLQDLR SQRHTEIDYI TGYLLRRARS HGMALPENAR LYELIKRKES DYERIGAGLP
GSW