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 A9BCT3

Entry ID Method Resolution Chain Position Source
AF-A9BCT3-F1 Predicted AlphaFoldDB

No variants for A9BCT3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A9BCT3

No associated diseases with A9BCT3

5 regional properties for A9BCT3

Type Name Position InterPro Accession
domain AAA+ ATPase domain 172 - 311 IPR003593
domain ATPase, AAA-type, core 176 - 309 IPR003959
conserved_site ATPase, AAA-type, conserved site 279 - 297 IPR003960
domain Proteasomal ATPase OB C-terminal domain 64 - 118 IPR032501
domain AAA ATPase, AAA+ lid domain 331 - 373 IPR041569

Functions

Description
EC Number 1.3.7.2 With an iron-sulfur protein as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
15,16-dihydrobiliverdin:ferredoxin oxidoreductase activity Catalysis of the reaction: 15,16-dihydrobiliverdin + oxidized ferredoxin = biliverdin IXa + reduced ferredoxin.
cobalt ion binding Binding to a cobalt ion (Co).

1 GO annotations of biological process

Name Definition
phytochromobilin biosynthetic process The chemical reactions and pathways resulting in the formation of phytochromobilin, which involves the oxidative cleavage of heme by a heme oxygenase(HO) to form biliverdin IX alpha.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MFDPYLDELN KLLIVNHGEI LLVPDGLQEC YSKKQDAVIR SWLWSVPGFR RWRVTRMDVG
70 80 90 100 110 120
DKLQVFNSVA YPDYLNEQPI MGIDLLWFGI KNKLVAVLDF QPLVQEKSYF DRYYQGLKSL
130 140 150 160 170 180
KARYSDFNSK DNVRAYDLSN YFSPWVLLCK GDLFQASSSL PFVFSEFLNA YFDISNNFKK
190 200 210 220 230
YNSRIEPNRV KELQISYDIY SSAHDPAHGL FKSYFGKQWS ERFLKEFLFP HSIAKDKT