P08065

PR
Gene name
sdhA (citF, BSU28440)
Protein name
Succinate dehydrogenase flavoprotein subunit
Names
Species
Bacillus subtilis (strain 168)
KEGG Pathway
bsu:BSU28440
EC number
1.3.5.1: With a quinone or related compound as acceptor
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

393-462 (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 P08065

Entry ID Method Resolution Chain Position Source
AF-P08065-F1 Predicted AlphaFoldDB

1 variants for P08065

Variant ID(s) Position Change Description Diseaes Association Provenance
48 G>D a defective mutant [UniProt] No

No associated diseases with P08065

3 regional properties for P08065

Type Name Position InterPro Accession
binding_site Fumarate reductase/succinate dehydrogenase, FAD-binding site 39 - 48 IPR003952
domain FAD-dependent oxidoreductase 2, FAD binding domain 6 - 392 IPR003953
domain Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal 452 - 579 IPR015939

Functions

Description
EC Number 1.3.5.1 With a quinone or related compound as acceptor
Subcellular Localization
  • Cell membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Membrane raft ; Peripheral membrane protein
  • Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
membrane raft Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

4 GO annotations of molecular function

Name Definition
electron transfer activity Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
succinate dehydrogenase (ubiquinone) activity Catalysis of the reaction: succinate + ubiquinone = fumarate + ubiquinol.
succinate dehydrogenase activity Catalysis of the reaction: succinate + acceptor = fumarate + reduced acceptor.

2 GO annotations of biological process

Name Definition
anaerobic respiration The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which uses compounds other than oxygen (e.g. nitrate, sulfate) as the terminal electron acceptor.
tricarboxylic acid cycle A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSQSSIIVVG GGLAGLMATI KAAESGMAVK LFSIVPVKRS HSVCAQGGIN GAVNTKGEGD
70 80 90 100 110 120
SPWEHFDDTV YGGDFLANQP PVKAMCEAAP SIIHLLDRMG VMFNRTPEGL LDFRRFGGTQ
130 140 150 160 170 180
HHRTAYAGAT TGQQLLYALD EQVRRYEVAG LVTKYEGWEF LGAVLDDDRT CRGIVAQNLT
190 200 210 220 230 240
NMQIESFRSD AVIMATGGPG IIFGKSTNSM INTGSAASIV YQQGAYYANG EFIQIHPTAI
250 260 270 280 290 300
PGDDKLRLMS ESARGEGGRV WTYKDGKPWY FLEEKYPAYG NLVPRDIATR EIFDVCVNQK
310 320 330 340 350 360
LGINGENMVY LDLSHKDPKE LDIKLGGIIE IYEKFMGDDP RKLPMKIFPA VHYSMGGLWV
370 380 390 400 410 420
DYDQMTNIPG LFAAGECDYS MHGGNRLGAN SLLSAIYGGM VAGPNAVKYV NGLESSAEDM
430 440 450 460 470 480
SSSLFDAHVK KEEEKWADIM SMDGTENAYV LHKELGEWMT ANVTVVRHND KLLKTDDKIQ
490 500 510 520 530 540
ELMERFKKIN INDTTKWSNQ GAMFTRQFSN MLQLARVITL GAYNRNESRG AHYKPDYPER
550 560 570 580
NDDEWLKTTM AKHVSPYEAP EFEYQDVDVS LITPRKRDYS KKKVAK