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 Q1IDV2

Entry ID Method Resolution Chain Position Source
AF-Q1IDV2-F1 Predicted AlphaFoldDB

No variants for Q1IDV2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q1IDV2

No associated diseases with Q1IDV2

2 regional properties for Q1IDV2

Type Name Position InterPro Accession
active_site Phosphoenolpyruvate carboxylase, Lys active site 133 - 144 IPR018129
active_site Phosphoenolpyruvate carboxylase, His active site 533 - 545 IPR033129

Functions

Description
EC Number 4.1.1.31 Carboxy-lyases
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
magnesium ion binding Binding to a magnesium (Mg) ion.
phosphoenolpyruvate carboxylase activity Catalysis of the reaction: phosphate + oxaloacetate = phosphoenolpyruvate + HCO3-.

3 GO annotations of biological process

Name Definition
carbon fixation A metabolic process in which carbon (usually derived from carbon dioxide) is incorporated into organic compounds (usually carbohydrates).
oxaloacetate metabolic process The chemical reactions and pathways involving oxaloacetate, the anion of oxobutanedioic acid, an important intermediate in metabolism, especially as a component of the TCA cycle.
tricarboxylic acid cycle A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSDIDQRLRE DVHLLGELLG ETIRQQHGEA FLQKIEDIRH SAKADRRGEG EQLSSTLGDL
70 80 90 100 110 120
AEEDLLPVAR AFNQFLNLAN IAEQYQLIHR RDTDQPEPFE ARVLPELLAR LKAAGHGNDA
130 140 150 160 170 180
LARQLARLDI QLVLTAHPTE VARRTLIQKY DAIAAQLAAQ DHRDLIPAER QQVRERLRRL
190 200 210 220 230 240
IAEAWHTEEI RRTRPTPVDE AKWGFAVIEH SLWQAVPNHL RKVDKALFEA TGLRLPLESA
250 260 270 280 290 300
PVRFASWMGG DRDGNPNVTA AVTREVLLLA RWMAADLFLR DIDYLAAELS MQQASGALRE
310 320 330 340 350 360
QVGDSAEPYR ALLKQLRDRL RATRAWAHAS LAGPQPASAA VLVDNRDLIA PLELCYQSLH
370 380 390 400 410 420
ACGMGVIADG PLLDSLRRAV TFGLFLVRLD VRQDAARHRD ALSEITDYLG LGRYADWDEE
430 440 450 460 470 480
RRIEFLQHEL KNRRPLLPAH FKPAAETAEV LATCREIAAA PAASLGSYVI SMAGAASDVL
490 500 510 520 530 540
AVQLLLKEAG LTRPMRVVPL FETLADLDNA GPVMERLLGL PGYRAGLHGP QEVMIGYSDS
550 560 570 580 590 600
AKDAGTTAAA WAQYRAQENL VRICREHQVE LLLFHGRGGT VGRGGGPAHA AILSQPPGSV
610 620 630 640 650 660
GGRFRTTEQG EMIRFKFGLP GIAEQNLNLY LAAVLEATLL PPPPPEPAWR ALMDQLAADG
670 680 690 700 710 720
VKAYRGVVRD NPEFVEYFRQ STPEQELGRL PLGSRPAKRR AGGIESLRAI PWIFGWTQTR
730 740 750 760 770 780
LMLPAWLGWE TALSNALARG QADLLAQMRE QWPFFRTRID MLEMVLAKAD AQIAEAYDQR
790 800 810 820 830 840
LVQPRLLPLG AHLRDLLSQS CQVVLGLTGQ QVLLAHSPET LEFIRLRNTY LDPLHRLQAE
850 860 870
LLARSRSREA ALDSPLEQAL LVTVAGIAAG LRNTG