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 P0ACB4

Entry ID Method Resolution Chain Position Source
AF-P0ACB4-F1 Predicted AlphaFoldDB

No variants for P0ACB4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P0ACB4

No associated diseases with P0ACB4

3 regional properties for P0ACB4

Type Name Position InterPro Accession
conserved_site Flavodoxin, conserved site 5 - 21 IPR001226
domain Flavodoxin/nitric oxide synthase 3 - 172 IPR008254
domain Flavodoxin domain 4 - 152 IPR026816

Functions

Description
EC Number 1.3.5.3 With a quinone or related compound as acceptor
Subcellular Localization
  • Cell inner membrane ; Peripheral membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
extrinsic component of cytoplasmic side of plasma membrane The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

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.
FMN binding Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
menaquinone-dependent protoporphyrinogen oxidase activity Catalysis of the reaction: protoporphyrinogen IX + menaquinone = protoporphyrin IX + reduced menaquinone.
oxygen-dependent protoporphyrinogen oxidase activity Catalysis of the reaction: 3 O(2) + protoporphyrinogen IX = 3 H(2)O(2) + protoporphyrin IX.

4 GO annotations of biological process

Name Definition
heme B biosynthetic process The chemical reactions and pathways resulting in the formation of heme B, a Fe(II) porphyrin complex readily isolated from the hemoglobin of beef blood, but also found in other proteins including other hemoglobins, myoglobins, cytochromes P-450, catalases, peroxidases as well as b type cytochromes.
heme biosynthetic process The chemical reactions and pathways resulting in the formation of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, from less complex precursors.
porphyrin-containing compound biosynthetic process The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
protoporphyrinogen IX biosynthetic process The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKTLILFSTR DGQTREIASY LASELKELGI QADVANVHRI EEPQWENYDR VVIGASIRYG
70 80 90 100 110 120
HYHSAFQEFV KKHATRLNSM PSAFYSVNLV ARKPEKRTPQ TNSYARKFLM NSQWRPDRCA
130 140 150 160 170 180
VIAGALRYPR YRWYDRFMIK LIMKMSGGET DTRKEVVYTD WEQVANFARE IAHLTDKPTL
K