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 P54822

Entry ID Method Resolution Chain Position Source
AF-P54822-F1 Predicted AlphaFoldDB

28 variants for P54822

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389354940 2 A>T No EVA
rs249386877 4 S>A No EVA
rs3389380547 23 S>N No EVA
rs217152533 28 F>L No EVA
rs3406374703 54 G>D No EVA
rs3406374653 62 I>T No EVA
rs3406416840 116 G>* No EVA
rs3406298395 116 G>A No EVA
rs3389337738 178 D>E No EVA
rs3389337797 223 D>G No EVA
rs3389378220 224 K>M No EVA
rs3389344607 236 F>I No EVA
rs3389294700 249 I>F No EVA
rs3389294700 249 I>V No EVA
rs3389378213 255 L>V No EVA
rs3389369425 281 P>S No EVA
rs3389369760 294 Y>* No EVA
rs3389385541 330 T>I No EVA
rs3389369749 344 A>E No EVA
rs3389337718 393 G>R No EVA
rs3389337711 406 L>F No EVA
rs3389327599 416 Q>* No EVA
rs3389365409 425 E>D No EVA
rs212437112 428 R>Q No EVA
rs3389344643 434 S>T No EVA
rs3389385555 448 S>F No EVA
rs3389354884 452 R>* No EVA
rs3389369440 457 V>L No EVA

No associated diseases with P54822

3 regional properties for P54822

Type Name Position InterPro Accession
domain Adenylosuccinate lyase C-terminal 377 - 461 IPR019468
conserved_site Fumarate lyase, conserved site 288 - 297 IPR020557
domain Fumarate lyase, N-terminal 99 - 308 IPR022761

Functions

Description
EC Number 4.3.2.2 Lyases acting on amides, amidines, etc
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.

3 GO annotations of molecular function

Name Definition
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity Catalysis of the reaction: (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
identical protein binding Binding to an identical protein or proteins.
N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity Catalysis of the reaction: N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP.

13 GO annotations of biological process

Name Definition
'de novo' AMP biosynthetic process The chemical reactions and pathways resulting in the formation of adenosine monophosphate (AMP) from inosine 5'-monophosphate (IMP).
'de novo' IMP biosynthetic process The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate.
'de novo' XMP biosynthetic process The chemical reactions and pathways resulting in the formation of XMP, xanthosine monophosphate, from simpler precursors.
aerobic respiration The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which requires oxygen as the terminal electron acceptor.
AMP biosynthetic process The chemical reactions and pathways resulting in the formation of AMP, adenosine monophosphate.
AMP salvage The chemical reactions and pathways resulting in the formation of adenosine monophosphate (AMP) from derivatives of it (either adenine, ADP or adenosine 3',5'-bisphosphate) without de novo synthesis.
GMP biosynthetic process The chemical reactions and pathways resulting in the formation of GMP, guanosine monophosphate.
purine nucleotide metabolic process The chemical reactions and pathways involving a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
response to hypoxia Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
response to muscle activity Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a muscle activity stimulus.
response to nutrient Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nutrient stimulus.
response to starvation Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a starvation stimulus, deprivation of nourishment.
ribonucleoside monophosphate biosynthetic process The chemical reactions and pathways resulting in the formation of a ribonucleoside monophosphate, a compound consisting of a nucleobase linked to a ribose sugar esterified with phosphate on the sugar.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q05911 ADE13 Adenylosuccinate lyase Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P21265 ADSL Adenylosuccinate lyase Gallus gallus (Chicken) PR
P30566 ADSL Adenylosuccinate lyase Homo sapiens (Human) PR
10 20 30 40 50 60
MAASGDPGSA ESYRSPLAAR YASREMCFLF SDRYKFQTWR QLWLWLAEAE QTLGLPITDE
70 80 90 100 110 120
QIQEMKSNLN NIDFQMAAEE EKRLRHDVMA HVHTFGHCCP KAAGIIHLGA TSCYVGDNTD
130 140 150 160 170 180
LIILRNAFDL LLPKLARVIS RLADFAKDRA DLPTLGFTHF QPAQLTTVGK RCCLWIQDLC
190 200 210 220 230 240
MDLQNLKRVR DELRFRGVKG TTGTQASFLQ LFEGDHQKVE QLDKMVTEKA GFKRAFIITG
250 260 270 280 290 300
QTYTRKVDIE VLSVLASLGA SVHKICTDIR LLANLKEMEE PFEKQQIGSS AMPYKRNPMR
310 320 330 340 350 360
SERCCSLARH LMALTMDPLQ TASVQWFERT LDDSANRRIC LAEAFLTADT ILNTLQNISE
370 380 390 400 410 420
GLVVYPKVIE RRIRQELPFM ATENIIMAMV KAGGSRQDCH EKIRVLSQQA AAVVKQEGGD
430 440 450 460 470 480
NDLIERIRAD AYFSPIHSQL EHLLDPSSFT GRAPQQVHRF LEEEVRPLLK PYGNEMAVKA
ELCL