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 Q99MN9

Entry ID Method Resolution Chain Position Source
AF-Q99MN9-F1 Predicted AlphaFoldDB

33 variants for Q99MN9

Variant ID(s) Position Change Description Diseaes Association Provenance
rs219459016 17 S>G No EVA
rs260077887 27 T>A No EVA
rs3389054688 40 R>H No EVA
rs260648302 73 S>R No EVA
rs3389064908 78 P>S No EVA
rs13469050 82 M>V No EVA
rs3389045597 139 H>Y No EVA
rs3389067672 142 K>R No EVA
rs3389045549 151 I>V No EVA
rs3400040395 162 D>E No EVA
rs3400650227 163 S>P No EVA
rs3389062009 172 V>M No EVA
rs3389068625 205 G>E No EVA
rs3400818785 218 M>I No EVA
rs3400818822 218 M>T No EVA
rs3400664913 219 V>M No EVA
rs3400818103 295 D>V No EVA
rs3389067705 310 L>F No EVA
rs3389059079 327 D>N No EVA
rs3389034136 345 G>D No EVA
rs3389034220 348 R>SE* No EVA
rs3389059118 349 M>V No EVA
rs3389064727 363 V>G No EVA
rs3389053358 375 K>N No EVA
rs3389032767 389 P>S No EVA
rs3389066590 428 K>Q No EVA
rs3389053414 441 Y>* No EVA
rs3389068623 446 S>F No EVA
rs3389032760 483 A>V No EVA
rs3389010693 497 P>R No EVA
rs3389045587 499 A>T No EVA
rs3389068703 510 P>S No EVA
rs3389068690 511 S>F No EVA

No associated diseases with Q99MN9

3 regional properties for Q99MN9

Type Name Position InterPro Accession
domain Acetyl-coenzyme A carboxyltransferase, N-terminal 34 - 292 IPR011762
domain Acetyl-coenzyme A carboxyltransferase, C-terminal 296 - 535 IPR011763
domain Acetyl-CoA carboxylase 60 - 539 IPR034733

Functions

Description
EC Number 6.4.1.3 Forming carbon-carbon bonds
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
catalytic complex A protein complex which is capable of catalytic 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.
propionyl-CoA carboxylase activity Catalysis of the reaction: ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

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
P34385 F02A9.10 Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial Caenorhabditis elegans PR
10 20 30 40 50 60
MAAAIRIRAV AAGARLSVLN CGLGITTRGL CSQPVSVKER IDNKRHAALL GGGQRRIDAQ
70 80 90 100 110 120
HKRGKLTARE RISLLLDPGS FMESDMFVEH RCADFGMAAD KNKFPGDSVV TGRGRINGRL
130 140 150 160 170 180
VYVFSQDFTV FGGSLSGAHA QKICKIMDQA ITVGAPVIGL NDSGGARIQE GVESLAGYAD
190 200 210 220 230 240
IFLRNVTASG VIPQISLIMG PCAGGAVYSP ALTDFTFMVK DTSYLFITGP EVVKSVTNED
250 260 270 280 290 300
VTQEQLGGAK THTTVSGVAH RAFDNDVDAL CNLREFFNFL PLSSQDPAPI RECHDPSDRL
310 320 330 340 350 360
VPELDTVVPL ESSKAYNMLD IIHAVIDERE FFEIMPSYAK NIVVGFARMN GRTVGIVGNQ
370 380 390 400 410 420
PNVASGCLDI NSSVKGARFV RFCDAFNIPL ITFVDVPGFL PGTAQEYGGI IRHGAKLLYA
430 440 450 460 470 480
FAEATVPKIT VITRKAYGGA YDVMSSKHLL GDTNYAWPTA EIAVMGAKGA VEIIFKGHQD
490 500 510 520 530 540
VEAAQAEYVE KFANPFPAAV RGFVDDIIQP SSTRARICCD LEVLASKKVH RPWRKHANIP
L