P00829

PR
Gene name
ATP5F1B
Protein name
ATP synthase subunit beta, mitochondrial
Names
ATP synthase F1 subunit beta
Species
Bos taurus (Bovine)
KEGG Pathway
bta:327675
EC number
7.1.2.2: Hydron translocation linked to the hydrolysis of a nucleoside triphosphate
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-86 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

55 structures for P00829

Entry ID Method Resolution Chain Position Source
1BMF X-ray 285 A D/E/F 47-528 PDB
1COW X-ray 310 A D/E/F 47-528 PDB
1E1Q X-ray 261 A D/E/F 47-528 PDB
1E1R X-ray 250 A D/E/F 47-528 PDB
1E79 X-ray 240 A D/E/F 47-528 PDB
1EFR X-ray 310 A D/E/F 47-528 PDB
1H8E X-ray 200 A D/E/F 47-528 PDB
1H8H X-ray 290 A D/E/F 47-528 PDB
1NBM X-ray 300 A D/E/F 47-526 PDB
1OHH X-ray 280 A D/E/F 47-528 PDB
1QO1 X-ray 390 A D/E/F 47-525 PDB
1W0J X-ray 220 A D/E/F 47-528 PDB
1W0K X-ray 285 A D/E/F 47-528 PDB
2CK3 X-ray 190 A D/E/F 47-528 PDB
2JDI X-ray 190 A D/E/F 47-528 PDB
2JIZ X-ray 230 A D/E/F/K/L/M 47-528 PDB
2JJ1 X-ray 270 A D/E/F/K/L/M 47-528 PDB
2JJ2 X-ray 240 A D/E/F/K/L/M 47-528 PDB
2V7Q X-ray 210 A D/E/F 47-528 PDB
2W6E X-ray 650 A D/E/F 1-528 PDB
2W6F X-ray 600 A D/E/F 1-528 PDB
2W6G X-ray 600 A D/E/F 1-528 PDB
2W6H X-ray 500 A D/E/F 1-528 PDB
2W6I X-ray 400 A D/E/F 1-528 PDB
2W6J X-ray 384 A D/E/F 1-528 PDB
2WSS X-ray 320 A D/E/F/M/N/O 47-528 PDB
2XND X-ray 350 A D/E/F 59-525 PDB
4ASU X-ray 260 A D/E/F 49-528 PDB
4TSF X-ray 320 A D/E/F 49-528 PDB
4TT3 X-ray 321 A D/E/F 49-528 PDB
4YXW X-ray 310 A D/E/F 47-528 PDB
4Z1M X-ray 330 A D/E/F 47-528 PDB
5ARA EM 670 A D/E/F 47-528 PDB
5ARE EM 740 A D/E/F 47-528 PDB
5ARH EM 720 A D/E/F 47-528 PDB
5ARI EM 740 A D/E/F 47-528 PDB
5FIJ EM 740 A D/E/F 47-528 PDB
5FIK EM 640 A D/E/F 47-528 PDB
5FIL EM 710 A D/E/F 47-528 PDB
6YY0 EM 323 A D/E/F 47-528 PDB
6Z1R EM 329 A D/E/F 47-528 PDB
6Z1U EM 347 A D/E/F 47-528 PDB
6ZPO EM 400 A D/E/F 47-528 PDB
6ZQM EM 329 A D/E/F 47-528 PDB
6ZQN EM 400 A D/E/F 47-528 PDB
7AJB EM 920 A AD/AE/AF/D/E/F 47-528 PDB
7AJC EM 1190 A AD/AE/AF/D/E/F 47-528 PDB
7AJD EM 900 A AD/AE/AF/D/E/F 47-528 PDB
7AJE EM 940 A AD/AE/AF/D/E/F 47-528 PDB
7AJF EM 845 A AD/AE/AF/D/E/F 47-528 PDB
7AJG EM 1070 A AD/AE/AF/D/E/F 47-528 PDB
7AJH EM 970 A AD/AE/AF/D/E/F 47-528 PDB
7AJI EM 1140 A AD/AE/AF/D/E/F 47-528 PDB
7AJJ EM 1310 A AD/AE/AF/D/E/F 47-528 PDB
AF-P00829-F1 Predicted AlphaFoldDB

1 variants for P00829

Variant ID(s) Position Change Description Diseaes Association Provenance
49 Q>del some mature chains [UniProt] No

No associated diseases with P00829

4 regional properties for P00829

Type Name Position InterPro Accession
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain 186 - 405 IPR000194
domain AAA+ ATPase domain 198 - 382 IPR003593
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain 63 - 129 IPR004100
active_site ATPase, alpha/beta subunit, nucleotide-binding domain, active site 396 - 405 IPR020003

Functions

Description
EC Number 7.1.2.2 Hydron translocation linked to the hydrolysis of a nucleoside triphosphate
Subcellular Localization
  • Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
mitochondrial proton-transporting ATP synthase complex A proton-transporting ATP synthase complex found in the mitochondrial membrane.
proton-transporting ATP synthase complex, catalytic core F(1) The sector of a hydrogen-transporting ATP synthase complex in which the catalytic activity resides; it comprises the catalytic core and central stalk, and is peripherally associated with a membrane, such as the plasma membrane or the mitochondrial inner membrane, when the entire ATP synthase is assembled.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
proton-transporting ATP synthase activity, rotational mechanism Enables the synthesis of ATP from ADP and phosphate by the transfer of protons from one side of a membrane to the other by a rotational mechanism driven by a gradient according to the reaction: ADP + H2O + phosphate + H+(in) -> ATP + H+(out).
proton-transporting ATPase activity, rotational mechanism Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) = ADP + phosphate + H+(out), by a rotational mechanism.

1 GO annotations of biological process

Name Definition
proton motive force-driven mitochondrial ATP synthesis The transport of protons across a mitochondrial membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5ZLC5 ATP5F1B ATP synthase subunit beta, mitochondrial Gallus gallus (Chicken) PR
Q05825 ATPsynbeta ATP synthase subunit beta, mitochondrial Drosophila melanogaster (Fruit fly) PR
P06576 ATP5F1B ATP synthase subunit beta, mitochondrial Homo sapiens (Human) PR
P56480 Atp5f1b ATP synthase subunit beta, mitochondrial Mus musculus (Mouse) PR
P10719 Atp5f1b ATP synthase subunit beta, mitochondrial Rattus norvegicus (Rat) PR
P46561 atp-2 ATP synthase subunit beta, mitochondrial Caenorhabditis elegans PR
10 20 30 40 50 60
MLGLVGRVVA ASASGALRGL SPSAPLPQAQ LLLRAAPAAL QPARDYAAQA SPSPKAGATT
70 80 90 100 110 120
GRIVAVIGAV VDVQFDEGLP PILNALEVQG RETRLVLEVA QHLGESTVRT IAMDGTEGLV
130 140 150 160 170 180
RGQKVLDSGA PIRIPVGPET LGRIMNVIGE PIDERGPIKT KQFAAIHAEA PEFVEMSVEQ
190 200 210 220 230 240
EILVTGIKVV DLLAPYAKGG KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT
250 260 270 280 290 300
REGNDLYHEM IESGVINLKD ATSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD
310 320 330 340 350 360
VLLFIDNIFR FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK KGSITSVQAI
370 380 390 400 410 420
YVPADDLTDP APATTFAHLD ATTVLSRAIA ELGIYPAVDP LDSTSRIMDP NIVGSEHYDV
430 440 450 460 470 480
ARGVQKILQD YKSLQDIIAI LGMDELSEED KLTVSRARKI QRFLSQPFQV AEVFTGHLGK
490 500 510 520
LVPLKETIKG FQQILAGEYD HLPEQAFYMV GPIEEAVAKA DKLAEEHS