Q5R7B3

PR
Gene name
UGDH
Protein name
UDP-glucose 6-dehydrogenase
Names
UDP-Glc dehydrogenase, UDP-GlcDH, UDPGDH
Species
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
KEGG Pathway
pon:100174620
EC number
1.1.1.22: 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)

438-494 (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 Q5R7B3

Entry ID Method Resolution Chain Position Source
AF-Q5R7B3-F1 Predicted AlphaFoldDB

No variants for Q5R7B3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5R7B3

No associated diseases with Q5R7B3

3 regional properties for Q5R7B3

Type Name Position InterPro Accession
domain UDP-glucose/GDP-mannose dehydrogenase, N-terminal 6 - 190 IPR001732
domain UDP-glucose/GDP-mannose dehydrogenase, dimerisation 214 - 308 IPR014026
domain UDP-glucose/GDP-mannose dehydrogenase, C-terminal 332 - 447 IPR014027

Functions

Description
EC Number 1.1.1.22 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

2 GO annotations of molecular function

Name Definition
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.
UDP-glucose 6-dehydrogenase activity Catalysis of the reaction: H(2)O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate.

7 GO annotations of biological process

Name Definition
carbohydrate metabolic process The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
chondroitin sulfate biosynthetic process The chemical reactions and pathways resulting in the formation of chondroitin sulfate, any member of a group of 10-60 kDa glycosaminoglycans, widely distributed in cartilage and other mammalian connective tissues, the repeat units of which consist of beta-(1,4)-linked D-glucuronyl beta-(1,3)-N-acetyl-D-galactosamine sulfate.
gastrulation with mouth forming second A gastrulation process in which the initial invagination becomes the anus and the mouth forms second.
heparan sulfate proteoglycan biosynthetic process The chemical reactions and pathways resulting in the formation of the heparan sulfate proteoglycan, a glycosaminoglycan with repeat unit consisting of alternating alpha-(1->4)-linked hexuronic acid and glucosamine residues; the former are a mixture of sulfated and nonsulfated D-glucuronic acid and L-iduronic acid; the L-iduronic acid is either sulfated or acetylated on its amino group as well as being sulfated on one of its hydroxyl groups; heparan sulfate chains are covalently linked to peptidyl-serine by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylosyl to serine residues.
neuron development The process whose specific outcome is the progression of a neuron over time, from initial commitment of the cell to a specific fate, to the fully functional differentiated cell.
protein hexamerization The formation of a protein hexamer, a macromolecular structure consisting of six noncovalently associated identical or nonidentical subunits.
UDP-glucuronate biosynthetic process The chemical reactions and pathways resulting in the formation of UDP-glucuronate, a substance composed of glucuronic acid in glycosidic linkage with uridine diphosphate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MFEIKKICCI GAGYVGGPTC SVIAHMRPEI RVTVVDVNES RINAWNSPTL PIYEPGLKEV
70 80 90 100 110 120
VESCRGKNLF FSTNIDDAIK EADLVFISVN TPTKTYGMGK GRAADLKYIE ACARRIVQNS
130 140 150 160 170 180
NGYKIVTEKS TVPVRAAESI RRIFDANTKP NLNLQVLSNP EFLAEGTAIK DLKNPDRVLI
190 200 210 220 230 240
GGDETPEGQR AVQALCAVYE HWVPREKILT TNTWSSELSK LAANAFLAQR ISSINSISAL
250 260 270 280 290 300
CEATGADVEE VATAIGMDQR IGNKFLKASV GFGGSCFQKD VLNLVYLCEA LNLPEVARYW
310 320 330 340 350 360
QQVIDMNDYQ RRRFASRIID SLFNTVTDKK IAILGFAFKK DTGDTRESSS IYISKYLMDE
370 380 390 400 410 420
GAHLHIYDPK VPREQIVVDL SHPGVSEDDQ VSRLVTISKD PYEACDGAHA VVICTEWDMF
430 440 450 460 470 480
KELDYERIHK KMLKPAFIFD GRRVLDGLHN ELQTIGFQIE TIGKKVSSKR IPYAPSGEIP
490
KFSLQDPPNK KPKV