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 Q8TL41

Entry ID Method Resolution Chain Position Source
AF-Q8TL41-F1 Predicted AlphaFoldDB

No variants for Q8TL41

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8TL41

No associated diseases with Q8TL41

1 regional properties for Q8TL41

Type Name Position InterPro Accession
conserved_site Histidinol dehydrogenase, conserved site 230 - 262 IPR001692

Functions

Description
EC Number 1.1.1.23 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
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.

3 GO annotations of molecular function

Name Definition
histidinol dehydrogenase activity Catalysis of the reaction: L-histidinol + NAD+ = L-histidine + NADH + H+.
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.
zinc ion binding Binding to a zinc ion (Zn).

1 GO annotations of biological process

Name Definition
histidine biosynthetic process The chemical reactions and pathways resulting in the formation of histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVTMLFKKLS DASEAEMKKL ISRGSGLADV GETVSSVLSD VRVRGDAALR EYTKKFDKVE
70 80 90 100 110 120
LAGFEVSEAE FEEALSGVGP ELLEHLKVAA ANIRVFHEAQ LPETTWFMEV QPGVVLGQKA
130 140 150 160 170 180
TALESVGAYA PGGRASYPST VLMTVIPARV AGVKQVIVCT PPRADGSIHP LTLAAAKVAG
190 200 210 220 230 240
ADKVFKLGGV QAVGAMAYGT ETVPKVDKIV GPGNVFVTSA KMQVRNVAEI DFPAGPSEVL
250 260 270 280 290 300
IIADDSADAA MVASDIIAQA EHDPNAVSVL VTTSEILAEA VRQEVLLQAE NTARSEIVKT
310 320 330 340 350 360
SLENAAVLIS DTLEQSIDFS NKFAPEHLEI MVEDSDFVLN RIKNAGSIFV GNYAPVPVGD
370 380 390 400 410 420
YASGTNHVLP TAGYARIYSG LNINHFLKYS SIQKISKSGL ESLKETIIAL AEEEGLQAHA
430
DAIRTRFGYK PSK