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 P34385

Entry ID Method Resolution Chain Position Source
AF-P34385-F1 Predicted AlphaFoldDB

No variants for P34385

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P34385

No associated diseases with P34385

3 regional properties for P34385

Type Name Position InterPro Accession
domain Acetyl-coenzyme A carboxyltransferase, N-terminal 94 - 351 IPR011762
domain Acetyl-coenzyme A carboxyltransferase, C-terminal 351 - 600 IPR011763
domain Acetyl-CoA carboxylase 120 - 604 IPR034733

Functions

Description
EC Number 6.4.1.4 Forming carbon-carbon bonds
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
methylcrotonoyl-CoA carboxylase complex A protein complex which is capable of methylcrotonoyl-CoA carboxylase activity.
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
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.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
methylcrotonoyl-CoA carboxylase activity Catalysis of the reaction: 3-methylbut-2-enoyl-CoA + ATP + bicarbonate = trans-3-methylglutaconyl-CoA + ADP + 2 H(+) + phosphate.

1 GO annotations of biological process

Name Definition
leucine catabolic process The chemical reactions and pathways resulting in the breakdown of leucine, 2-amino-4-methylpentanoic acid.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9V9A7 Mccc2 Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial Drosophila melanogaster (Fruit fly) PR
Q99MN9 Pccb Propionyl-CoA carboxylase beta chain, mitochondrial Mus musculus (Mouse) PR
10 20 30 40 50 60
MFRHVAQNLG SRNTSIQSYR LLRTRWERGY LKDLYHRRQI LGADPAISRS SYPNCSVQVR
70 80 90 100 110 120
NHHCSADKST LQWAPIKTSI DNSSDDFAAN TAEMKVLVED LKAKISKIEQ AGGEKAVKLH
130 140 150 160 170 180
RSRGKMLARE RIDGIVDAGS PFIEFSQLAG YEMYGKEEVP SGGILTGVGI VSGRVCVIVA
190 200 210 220 230 240
NDATVKGGTY YPITVKKHLR AQEIARENKL PCIYLVDSGG ANLPRQADIF ADSQHFGRIF
250 260 270 280 290 300
YNQATMSSEG IPQLAVVMGS CTAGGAYVPA MSDQAIIVKG TGTVFLGGPP LVKAATGEEI
310 320 330 340 350 360
SAEELGGADL HCGESGVTDY YAHNDKHALY LARSCIAGLP PVEEHMTFNP NADEPLYPAE
370 380 390 400 410 420
EIYGIVGSNL KKTYDVREVI ARIVDGSRFH EFKERYGETL VTGFATIYGQ RVGILANNGV
430 440 450 460 470 480
LFAESAMKGS HFIELCCQRK IPLLFLQNIT GFMVGRDAEA GGIAKHGAKL VTAVACAKVP
490 500 510 520 530 540
KITVLVGGSY GAGNYGMCGR GYSPRYVFMW PNSRISVMGG EQAANVLSTV QKEKKKREGA
550 560 570 580 590 600
DWTDQQDLEL RKPVEEKFEK EGHPYFASAR LWDDGVIDPK DTRKVLGLAF QSTLQKPIPE
TKFGVFRM