P11497

PR
Gene name
Acaca
Protein name
Acetyl-CoA carboxylase 1
Names
ACC1, ACC-alpha
Species
Rattus norvegicus (Rat)
KEGG Pathway
rno:60581
EC number
6.4.1.2: Forming carbon-carbon bonds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1162-1236 (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 P11497

Entry ID Method Resolution Chain Position Source
AF-P11497-F1 Predicted AlphaFoldDB

No variants for P11497

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P11497

No associated diseases with P11497

11 regional properties for P11497

Type Name Position InterPro Accession
domain Biotin/lipoyl attachment 744 - 818 IPR000089
binding_site Biotin-binding site 775 - 792 IPR001882
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 287 - 469 IPR005479
domain Biotin carboxylase-like, N-terminal domain 117 - 236 IPR005481
domain Biotin carboxylase, C-terminal 506 - 613 IPR005482
domain ATP-grasp fold 274 - 465 IPR011761
domain Acetyl-coenzyme A carboxyltransferase, N-terminal 1575 - 1913 IPR011762
domain Acetyl-coenzyme A carboxyltransferase, C-terminal 1917 - 2233 IPR011763
domain Biotin carboxylation domain 116 - 617 IPR011764
domain Acetyl-CoA carboxylase, central domain 818 - 1568 IPR013537
domain Acetyl-CoA carboxylase 1668 - 2221 IPR034733

Functions

Description
EC Number 6.4.1.2 Forming carbon-carbon bonds
Subcellular Localization
  • Cytoplasm, cytosol
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 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.

5 GO annotations of molecular function

Name Definition
acetyl-CoA carboxylase activity Catalysis of the reaction: ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
biotin binding Binding to biotin (cis-tetrahydro-2-oxothieno(3,4-d)imidazoline-4-valeric acid), the (+) enantiomer of which is very widely distributed in cells and serves as a carrier in a number of enzymatic beta-carboxylation reactions.
identical protein binding Binding to an identical protein or proteins.
metal ion binding Binding to a metal ion.

11 GO annotations of biological process

Name Definition
acetyl-CoA metabolic process The chemical reactions and pathways involving acetyl-CoA, a derivative of coenzyme A in which the sulfhydryl group is acetylated; it is a metabolite derived from several pathways (e.g. glycolysis, fatty acid oxidation, amino-acid catabolism) and is further metabolized by the tricarboxylic acid cycle. It is a key intermediate in lipid and terpenoid biosynthesis.
cellular response to prostaglandin E stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a prostagladin E stimulus.
fatty acid biosynthetic process The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
lipid homeostasis Any process involved in the maintenance of an internal steady state of lipid within an organism or cell.
lipid metabolic process The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
malonyl-CoA biosynthetic process The chemical reactions and pathways resulting in the formation of malonyl-CoA, the S-malonyl derivative of coenzyme A.
protein homotetramerization The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits.
protein metabolic process The chemical reactions and pathways involving a protein. Includes protein modification.
response to organic cyclic compound 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 an organic cyclic compound stimulus.
response to xenobiotic stimulus 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 from a xenobiotic, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.
tissue homeostasis A homeostatic process involved in the maintenance of an internal steady state within a defined tissue of an organism, including control of cellular proliferation and death and control of metabolic function.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P11029 ACAC Acetyl-CoA carboxylase Gallus gallus (Chicken) PR
O00763 ACACB Acetyl-CoA carboxylase 2 Homo sapiens (Human) PR
Q13085 ACACA Acetyl-CoA carboxylase 1 Homo sapiens (Human) PR
E9Q4Z2 Acacb Acetyl-CoA carboxylase 2 Mus musculus (Mouse) PR
Q5SWU9 Acaca Acetyl-CoA carboxylase 1 Mus musculus (Mouse) PR
10 20 30 40 50 60
MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP ASVSSDTLSD
70 80 90 100 110 120
LGISALQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT VASPAEFVTR FGGNKVIEKV
130 140 150 160 170 180
LIANNGIAAV KCMRSIRRWS YEMFRNERAI RFVVMVTPED LKANAEYIKM ADHYVPVPGG
190 200 210 220 230 240
ANNNNYANVE LILDIAKRIP VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG
250 260 270 280 290 300
DKIASSIVAQ TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA
310 320 330 340 350 360
EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL AKQSRHLEVQ
370 380 390 400 410 420
ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF EHMEQCAVKL AKMVGYVSAG
430 440 450 460 470 480
TVEYLYSQDG SFYFLELNPR LQVEHPCTEM VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG
490 500 510 520 530 540
VSPWGDAPID FENSAHVPCP RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF
550 560 570 580 590 600
SVAAAGGLHE FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE
610 620 630 640 650 660
SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VNLRNSISNF LHSLERGQVL
670 680 690 700 710 720
PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC VEVDVHRLSD GGLLLSYDGS
730 740 750 760 770 780
SYTTYMKEEV DRYRITIGNK TCVFEKENDP SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE
790 800 810 820 830 840
IEVMKMVMTL TAVESGCIHY VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS
850 860 870 880 890 900
TALRGEKLHR VFHYVLDNLV NVMNGYCLPD PFFSSKVKDW VERLMKTLRD PSLPLLELQD
910 920 930 940 950 960
IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT LNRKSEREVF
970 980 990 1000 1010 1020
FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF QNGHYDKCVF ALREENKSDM
1030 1040 1050 1060 1070 1080
NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR DPTLTDELLN ILTELTQLSK TTNAKVALRA
1090 1100 1110 1120 1130 1140
RQVLIASHLP SYDVRHNQVE SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS
1150 1160 1170 1180 1190 1200
NQVVRMAALE VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS
1210 1220 1230 1240 1250 1260
FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE VMGCFCDSPP
1270 1280 1290 1300 1310 1320
QSPTFPESGH TSLYDEDKVP RDEPIHILNV AIKTDGDIED DRLAAMFREF TQQNKATLVE
1330 1340 1350 1360 1370 1380
HGIRRLTFLV AQKDFRKQVN CEVDQRFHRE FPKFFTFRAR DKFEEDRIYR HLEPALAFQL
1390 1400 1410 1420 1430 1440
ELNRMRNFDL TAIPCANHKM HLYLGAAKVE VGTEVTDYRF FVRAIIRHSD LVTKEASFEY
1450 1460 1470 1480 1490 1500
LQNEGERLLL EAMDELEVAF NNTNVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS
1510 1520 1530 1540 1550 1560
RLWKLRVLQA ELKINIRLTT TGKAIPIRLF LTNESGYYLD ISLYKEVTDS RTAQIMFQAY
1570 1580 1590 1600 1610 1620
GDKQGPLHGM LINTPYVTKD LLQSKRFQAQ SLGTTYIYDI PEMFRQSLIK LWESMSTQAF
1630 1640 1650 1660 1670 1680
LPSPPLPSDI LTYTELVLDD QGQLVHMNRL PGGNEIGMVA WKMSLKSPEY PDGRDVIVIG
1690 1700 1710 1720 1730 1740
NDITYRIGSF GPQEDLLFLR ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDS
1750 1760 1770 1780 1790 1800
EDPYKGYKYL YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG
1810 1820 1830 1840 1850 1860
MIAGESSLAY DEIITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA GALNKVLGRE
1870 1880 1890 1900 1910 1920
VYTSNNQLGG IQIMHNNGVT HCTVCDDFEG VFTVLHWLSY MPKNVHSSVP LLNSKDPIDR
1930 1940 1950 1960 1970 1980
IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL SGFFDYGSFS EIMQPWAQTV VVGRARLGGI
1990 2000 2010 2020 2030 2040
PVGVVAVETR TVELSVPADP ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM
2050 2060 2070 2080 2090 2100
VFANWRGFSG GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN
2110 2120 2130 2140 2150 2160
PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL GTPELSPTER
2170 2180 2190 2200 2210 2220
KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV INDILDWKTS RTFFYWRLRR
2230 2240 2250 2260 2270 2280
LLLEDLVKKK IHSANPELTD GQIQAMLRRW FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE
2290 2300 2310 2320 2330 2340
DGVRSVIEEN IKYISRDYVL KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM
DSPST