P23704

PR
Gene name
atp-2 (B8B20.320, NCU05430)
Protein name
ATP synthase subunit beta, mitochondrial
Names
Species
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
KEGG Pathway
ncr:NCU05430
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)

1-64 (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 P23704

Entry ID Method Resolution Chain Position Source
AF-P23704-F1 Predicted AlphaFoldDB

No variants for P23704

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P23704

No associated diseases with P23704

4 regional properties for P23704

Type Name Position InterPro Accession
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain 175 - 393 IPR000194
domain AAA+ ATPase domain 187 - 370 IPR003593
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain 51 - 118 IPR004100
active_site ATPase, alpha/beta subunit, nucleotide-binding domain, active site 384 - 393 IPR020003

Functions

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

3 GO annotations of cellular component

Name Definition
mitochondrial proton-transporting ATP synthase complex A proton-transporting ATP synthase complex found in the mitochondrial membrane.
mitochondrial proton-transporting ATP synthase, catalytic core The hexamer, comprising three alpha and three beta subunits, that possesses the catalytic activity of the mitochondrial hydrogen-transporting ATP synthase.
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.

5 GO annotations of molecular function

Name Definition
ADP binding Binding to ADP, adenosine 5'-diphosphate.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MFKSGISAFA RTARPSFAAA SRRAVRPAAL NLRAPALSRF ASSAGVGDGK IYQVIGAVVD
70 80 90 100 110 120
VKFDTDKLPP ILNALETQNN GQKLVLEVSQ HLGENVVRCI AMDGTEGLVR GAKASDTGAP
130 140 150 160 170 180
ITIPVGPATL GRIINVTGDP IDERGPIKTD KFRPIHAEAP EFVEQSTTAE ILVTGIKVVD
190 200 210 220 230 240
LLAPYARGGK IGLFGGAGVG KTVFIQELIN NIAKAHGGYS VFTGVGERTR EGNDLYHEMQ
250 260 270 280 290 300
ETSVIQLDGD SKVALVFGQM NEPPGARARV ALTGLTIAEY FRDEEGQDVL LFIDNIFRFT
310 320 330 340 350 360
QAGSEVSALL GRIPSAVGYQ PTLAVDMGQM QERITTTTKG SITSVQAVYV PADDLTDPAP
370 380 390 400 410 420
ATTFAHLDAT TVLSRGISEL GIYPAVDPLD SKSRMLDPRI VGQEHYETAT RVQQILQEYK
430 440 450 460 470 480
SLQDIIAILG MDELSEADKL TVERARKIQR FLSQPFTVAQ VFTGIEGKLV DLKDTIASFK
490 500 510
AILAGEGDDL PEGAFYMVGD FASARAKGEK ILAELEGQA