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 A4YGR1

Entry ID Method Resolution Chain Position Source
AF-A4YGR1-F1 Predicted AlphaFoldDB

No variants for A4YGR1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A4YGR1

No associated diseases with A4YGR1

4 regional properties for A4YGR1

Type Name Position InterPro Accession
domain AMP-dependent synthetase/ligase domain 97 - 531 IPR000873
conserved_site AMP-binding, conserved site 264 - 275 IPR020845
domain AMP-binding enzyme, C-terminal domain 540 - 617 IPR025110
domain Acetyl-coenzyme A synthetase, N-terminal domain 31 - 85 IPR032387

Functions

Description
EC Number 6.2.1.36 Acid--thiol ligases
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

4 GO annotations of molecular function

Name Definition
3-hydroxypropionyl-CoA synthetase activity Catalysis of the reaction: 3-hydroxypropionate + ATP + CoA = 3-hydroxypropionyl-CoA + AMP + diphosphate.
acetate-CoA ligase activity Catalysis of the reaction: ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA.
AMP binding Binding to AMP, adenosine monophosphate.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

2 GO annotations of biological process

Name Definition
acetyl-CoA biosynthetic process from acetate The chemical reactions and pathways resulting in the formation of acetyl-CoA from acetate, either directly or via acetylphosphate.
carbon fixation by 3-hydroxypropionate cycle An autotrophic carbon dioxide fixation pathway by which two molecules of carbon dioxide are fixed to form glyoxylate. Acetyl coenzyme A (acetyl-CoA) is assumed to be converted to malate, and two CO2 molecules are thereby fixed. Malyl-CoA is thought to be cleaved to acetyl-CoA, the starting molecule, and glyoxylate, the carbon fixation product.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MFMRYIMVEE QTLKTGSQEL EEKADYNMRY YAHLMKLSKE KPAEFWGSLA QDLLDWYEPW
70 80 90 100 110 120
KETMRQEDPM TRWFIGGKIN ASYNAVDRHL NGPRKFKAAV IWESELGERK IVTYQDMFYE
130 140 150 160 170 180
VNRWANALRS LGVGKGDRVT IYMPLTPEGI AAMLASARIG AIHSVIFAGF GSQAIADRVE
190 200 210 220 230 240
DAKAKVVITA DAYPRRGKVV ELKKTVDEAL NSLGERSPVQ HVLVYRRMKT DVNMKEGRDV
250 260 270 280 290 300
FFDEVGKYRY VEPERMDSND PLFILYTSGT TGKPKGIMHS TGGYLTGTAV MLLWSYGLSQ
310 320 330 340 350 360
ENDVLFNTSD IGWIVGHSYI TYSPLIMGRT VVIYESAPDY PYPDKWAEII ERYRATTFGT
370 380 390 400 410 420
SATALRYFMK YGDEYVKNHD LSSIRIIVTN GEVLNYSPWK WGLEVLGGGK VFMSHQWWQT
430 440 450 460 470 480
ETGAPNLGYL PGIIYMPMKS GPASGFPLPG NFVEVLDENG NPSAPRVRGY LVMRPPFPPN
490 500 510 520 530 540
MMMGMWNDNG ERLKKTYFSK FGSLYYPGDF AMVDEDGYIW VLGRADETLK IAAHRIGAGE
550 560 570 580 590 600
VESAITSHPS VAEAAVIGVP DSVKGEEVHA FVVLKQGYAP SSELAKDIQS HVRKVMGPIV
610 620 630 640 650 660
SPQIHFVDKL PKTRSGKVMR RVIKAVMMGS SAGDLTTIED EASMDEIKKA VEELKKELKT
S