P9WJ92

PR
Gene name
hmp (kshB, MT3676)
Protein name
3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component
Names
3-ketosteroid-9-alpha-hydroxylase, ferredoxin reductase component, KSH, Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase, Rieske-type oxygenase, RO
Species
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
KEGG Pathway
mtc:MT3676
EC number
1.14.15.30: With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

224-299 (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 P9WJ92

Entry ID Method Resolution Chain Position Source
AF-P9WJ92-F1 Predicted AlphaFoldDB

No variants for P9WJ92

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P9WJ92

No associated diseases with P9WJ92

9 regional properties for P9WJ92

Type Name Position InterPro Accession
domain 2Fe-2S ferredoxin-type iron-sulfur binding domain 269 - 358 IPR001041
domain Oxidoreductase FAD/NAD(P)-binding 132 - 229 IPR001433
domain Flavoprotein pyridine nucleotide cytochrome reductase 72 - 79 IPR001709-1
domain Flavoprotein pyridine nucleotide cytochrome reductase 131 - 150 IPR001709-2
domain Flavoprotein pyridine nucleotide cytochrome reductase 155 - 164 IPR001709-3
domain Flavoprotein pyridine nucleotide cytochrome reductase 215 - 223 IPR001709-4
binding_site 2Fe-2S ferredoxin, iron-sulphur binding site 305 - 313 IPR006058
domain Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain 48 - 121 IPR008333
domain FAD-binding domain, ferredoxin reductase-type 12 - 124 IPR017927

Functions

Description
EC Number 1.14.15.30 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen
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

3 GO annotations of molecular function

Name Definition
2 iron, 2 sulfur cluster binding Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
3-ketosteroid 9-alpha-monooxygenase activity Catalysis of the reaction: androsta-1,4-diene-3,17-dione + NADH + H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O.
metal ion binding Binding to a metal ion.

3 GO annotations of biological process

Name Definition
cholesterol metabolic process The chemical reactions and pathways involving cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones. It is a component of the plasma membrane lipid bilayer and of plasma lipoproteins and can be found in all animal tissues.
lipid catabolic process The chemical reactions and pathways resulting in the breakdown of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.
steroid biosynthetic process The chemical reactions and pathways resulting in the formation of steroids, compounds with a 1,2,cyclopentanoperhydrophenanthrene nucleus; includes de novo formation and steroid interconversion by modification.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTEAIGDEPL GDHVLELQIA EVVDETDEAR SLVFAVPDGS DDPEIPPRRL RYAPGQFLTL
70 80 90 100 110 120
RVPSERTGSV ARCYSLCSSP YTDDALAVTV KRTADGYASN WLCDHAQVGM RIHVLAPSGN
130 140 150 160 170 180
FVPTTLDADF LLLAAGSGIT PIMSICKSAL AEGGGQVTLL YANRDDRSVI FGDALRELAA
190 200 210 220 230 240
KYPDRLTVLH WLESLQGLPS ASALAKLVAP YTDRPVFICG PGPFMQAARD ALAALKVPAQ
250 260 270 280 290 300
QVHIEVFKSL ESDPFAAVKV DDSGDEAPAT AVVELDGQTH TVSWPRTAKL LDVLLAAGLD
310 320 330 340 350
APFSCREGHC GACACTLRAG KVNMGVNDVL EQQDLDEGLI LACQSRPESD SVEVTYDE