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 Q465R4

Entry ID Method Resolution Chain Position Source
AF-Q465R4-F1 Predicted AlphaFoldDB

No variants for Q465R4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q465R4

No associated diseases with Q465R4

1 regional properties for Q465R4

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

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

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
MVMMLFKKLS DVSEAEMQKL LSRGSGLEDV AKTVSTVLSD VRTKGDSALR EYTAKFDKVE
70 80 90 100 110 120
LANFGVSEEE FQQALSGISP ELLDHLKSAA ANIRAFHEAQ LPKATWFMEL KPGIVLGQKA
130 140 150 160 170 180
TPLESVGAYA PGGRASYPST VLMTVIPARV AGVEQVIVCT PPRPDGSVHP LTLAAAKVAG
190 200 210 220 230 240
ADKVFKLGGV QAIGSMAYGT ETVPKVDKIV GPGNVFVTAA KMQIRDVAEI DFPAGPSEVL
250 260 270 280 290 300
IIADESADAV MVASDILAQS EHDPNSVSIL VTGSDTLAEA VKREVLVQAE QAARSSIIKS
310 320 330 340 350 360
SLENAAILIA DSLEQCIGFS NKFAPEHLEI MVADPDFVLD RIKNAGSIFI GNYSPVPVGD
370 380 390 400 410 420
YASGTNHVLP TSGYARVYSG LNINHFIKYS SIQRISKSGL ESLKETVIAL AEEEGLQAHA
430
DAIRTRFGYK PSK