Q9PTY0

PR
Gene name
ATP5F1B
Protein name
ATP synthase subunit beta, mitochondrial
Names
ATP synthase F1 subunit beta
Species
Cyprinus carpio (Common carp)
KEGG Pathway
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)

1-75 (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 Q9PTY0

Entry ID Method Resolution Chain Position Source
AF-Q9PTY0-F1 Predicted AlphaFoldDB

No variants for Q9PTY0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9PTY0

No associated diseases with Q9PTY0

4 regional properties for Q9PTY0

Type Name Position InterPro Accession
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain 176 - 395 IPR000194
domain AAA+ ATPase domain 188 - 372 IPR003593
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain 53 - 119 IPR004100
active_site ATPase, alpha/beta subunit, nucleotide-binding domain, active site 386 - 395 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

3 GO annotations of cellular component

Name Definition
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
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.
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.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
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.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLGAVGRCCT GALQALRPGV TPLKALNGAP AALFSRRDYV APAAAAAAAS GRIVAVIGAV
70 80 90 100 110 120
VDVQFDEDLP PILNALEVAG RDTRLVLEVA QHLGENTVRT IAMDGTEGLV RGQKVLDTGA
130 140 150 160 170 180
PIRIPVGPET LGRIMNVIGE PIDERGPITT KQTAPIHAEA PEFTDMSVEQ EILVTGIKVV
190 200 210 220 230 240
DLLAPYAKGG KIGLFGGAGV GKTVLIMELI NNVAKAHGGY SVFAGVGERT REGNDLYHEM
250 260 270 280 290 300
IESGVINLKD TTSKVALVYG QMNEPPGARA RVALTGLTVA EYFRDQEGQD VLLFIDNIFR
310 320 330 340 350 360
FTQAGSEVSA LLGRIPSAVG YQPTLATDMG TMQERITTTK KGSITSVQAI YVPADDLTDP
370 380 390 400 410 420
APATTFAHLD ATTVLSRAIA ELGIYPAVDP LDSTSRIMDP NIVGSEHYDV ARGVQKILQD
430 440 450 460 470 480
YKSLQDIIAI LGMDELSEED KLTVARARKI QRFLSQPFQV AEVFTGHLGK LVPLKDTIKG
490 500 510
FKAILGGEYD ALPEQAFYMV GPIEEVVQKA EKLAEEHS