UniProtKB - P71858 (CHSE2_MYCTU)
Protein
Acyl-CoA dehydrogenase FadE29
Gene
fadE29
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Involved in the third cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism (PubMed:26161441). Contributes partly to the virulence by increasing the efficiency of beta-oxidation (PubMed:22045806, PubMed:23560677). Catalyzes the dehydrogenation of 2'-propanoyl-CoA ester side chains of 3-oxo-4-pregnene-20-carboxyl-CoA (3-OPC-CoA) to yield 3-oxo-4,17-pregnadiene-20-carboxyl-CoA (3-OPDC-CoA). Also able to dehydrogenate steroyl-CoA such as 3-oxo-chol-4-en-24-oyl-CoA (3-OCO-CoA), 1beta-(2'-propanoyl-CoA)-3a-alpha-H- 7a-beta-methylhexahydro-4-indanone (indanone-CoA ester), hexahydroindanone and pregenenone (PubMed:22045806, PubMed:23560677).3 Publications
Catalytic activityi
Cofactori
FAD1 PublicationNote: Binds 1 FAD per heterodimer.1 Publication
Kineticsi
Kcat is 78 min(-1) for 3-OPC-CoA as substrate (at pH 8.5 and 25 degrees Celsius) (PubMed:23560677). Kcat is 5.1 min(-1) for indanone-CoA ester as substrate (at pH 8.5 and 25 degrees Celsius) (PubMed:23560677). Kcat is 1.3 sec(-1) for 3-OPC-CoA as substrate (at pH 8.5 and 25 degrees Celsius) (PubMed:26161441). Kcat is 0.16 sec(-1) for 3-OCO-CoA as substrate (at pH 8.5 and 25 degrees Celsius) (PubMed:26161441).2 Publications
- KM=5.3 µM for 3-OPC-CoA (at pH 8.5 and 25 degrees Celsius)2 Publications
- KM=6.5 µM for 3-OCO-CoA (at pH 8.5 and 25 degrees Celsius)1 Publication
- KM=86 µM for indanone-CoA ester (at pH 8.5 and 25 degrees Celsius)1 Publication
: cholesterol degradation Pathwayi
This protein is involved in the pathway cholesterol degradation, which is part of Steroid metabolism.1 PublicationView all proteins of this organism that are known to be involved in the pathway cholesterol degradation and in Steroid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 132 | FADBy similarity | 1 | |
Binding sitei | 158 | FADBy similarity | 1 | |
Active sitei | 241 | Proton acceptor1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 123 – 126 | FADBy similarity | 4 | |
Nucleotide bindingi | 367 – 369 | FADBy similarity | 3 |
GO - Molecular functioni
- FAD binding Source: UniProtKB
- oxidoreductase activity, acting on the CH-CH group of donors Source: InterPro
GO - Biological processi
- cholesterol catabolic process Source: UniProtKB
- fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: UniProtKB
- growth of symbiont in host Source: MTBBASE
- pathogenesis Source: UniProtKB-KW
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Cholesterol metabolism, Lipid degradation, Lipid metabolism, Steroid metabolism, Sterol metabolism, Virulence |
Ligand | FAD, Flavoprotein, NAD, NADP |
Enzyme and pathway databases
BioCyci | MetaCyc:G185E-7820-MONOMER |
UniPathwayi | UPA01058 |
Names & Taxonomyi
Protein namesi | Recommended name: Acyl-CoA dehydrogenase FadE291 Publication (EC:1.3.99.-2 Publications)Short name: ACAD1 Publication Alternative name(s): 3-oxo-23,24-bisnorchol-4-en-22-oyl-CoA dehydrogenase beta subunit1 Publication 3-oxo-4-pregnene-20-carboxyl-CoA dehydrogenase beta subunit1 Publication |
Gene namesi | Name:fadE29 Ordered Locus Names:Rv3543c |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv3543c |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 241 | E → Q: Unable to dehydrogenate pregnene-carboxyl-CoA ester. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000438518 | 1 – 387 | Acyl-CoA dehydrogenase FadE29Add BLAST | 387 |
Proteomic databases
PaxDbi | P71858 |
Expressioni
Inductioni
Induced by cholesterol and repressed by KtsR.1 Publication
Interactioni
Subunit structurei
Heterotetramer composed of FadE28 and FadE29.
2 PublicationsProtein-protein interaction databases
STRINGi | 83332.Rv3543c |
Family & Domainsi
Sequence similaritiesi
Belongs to the acyl-CoA dehydrogenase family.Curated
Phylogenomic databases
eggNOGi | COG1960, Bacteria |
InParanoidi | P71858 |
OMAi | VEQQIFV |
PhylomeDBi | P71858 |
Family and domain databases
Gene3Di | 1.10.540.10, 1 hit |
InterProi | View protein in InterPro IPR006091, Acyl-CoA_Oxase/DH_cen-dom IPR036250, AcylCo_DH-like_C IPR009075, AcylCo_DH/oxidase_C IPR013786, AcylCoA_DH/ox_N IPR037069, AcylCoA_DH/ox_N_sf IPR009100, AcylCoA_DH/oxidase_NM_dom |
Pfami | View protein in Pfam PF00441, Acyl-CoA_dh_1, 1 hit PF02770, Acyl-CoA_dh_M, 1 hit PF02771, Acyl-CoA_dh_N, 1 hit |
SUPFAMi | SSF47203, SSF47203, 1 hit SSF56645, SSF56645, 1 hit |
i Sequence
Sequence statusi: Complete.
P71858-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MFIDLTPEQR QLQAEIRQYF SNLISPDERT EMEKDRHGPA YRAVIRRMGR
60 70 80 90 100
DGRLGVGWPK EFGGLGFGPI EQQIFVNEAH RADVPLPAVT LQTVGPTLQA
110 120 130 140 150
HGSELQKKKF LPAILAGEAH FAIGYTEPEA GTDLASLRTT AVRDGDHYIV
160 170 180 190 200
NGQKVFTTGA HDADYIWLAC RTDPNAAKHK GISILIVDTK DPGYSWTPII
210 220 230 240 250
LADGAHHTNA TYYNDVRVPV DMLVGKENDG WRLITTQLNN ERVMLGPAGR
260 270 280 290 300
FASIYDRVHA WASVPGGNGV TPIDHDDVKR ALGEIRAIWR INELLNWQVA
310 320 330 340 350
SAGEDINMAD AAATKVFGTE RVQRAGRLAE EIVGKYGNPA EPDTAELLRW
360 370 380
LDAQTKRNLV ITFGGGVNEV MREMIAASGL KVPRVPR
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP46365.1 |
RefSeqi | NP_218060.1, NC_000962.3 WP_003419296.1, NZ_NVQJ01000014.1 |
Genome annotation databases
EnsemblBacteriai | CCP46365; CCP46365; Rv3543c |
GeneIDi | 23490183 888131 |
KEGGi | mtu:Rv3543c mtv:RVBD_3543c |
PATRICi | fig|83332.111.peg.3948 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP46365.1 |
RefSeqi | NP_218060.1, NC_000962.3 WP_003419296.1, NZ_NVQJ01000014.1 |
3D structure databases
SMRi | P71858 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv3543c |
Proteomic databases
PaxDbi | P71858 |
Genome annotation databases
EnsemblBacteriai | CCP46365; CCP46365; Rv3543c |
GeneIDi | 23490183 888131 |
KEGGi | mtu:Rv3543c mtv:RVBD_3543c |
PATRICi | fig|83332.111.peg.3948 |
Organism-specific databases
TubercuListi | Rv3543c |
Phylogenomic databases
eggNOGi | COG1960, Bacteria |
InParanoidi | P71858 |
OMAi | VEQQIFV |
PhylomeDBi | P71858 |
Enzyme and pathway databases
UniPathwayi | UPA01058 |
BioCyci | MetaCyc:G185E-7820-MONOMER |
Family and domain databases
Gene3Di | 1.10.540.10, 1 hit |
InterProi | View protein in InterPro IPR006091, Acyl-CoA_Oxase/DH_cen-dom IPR036250, AcylCo_DH-like_C IPR009075, AcylCo_DH/oxidase_C IPR013786, AcylCoA_DH/ox_N IPR037069, AcylCoA_DH/ox_N_sf IPR009100, AcylCoA_DH/oxidase_NM_dom |
Pfami | View protein in Pfam PF00441, Acyl-CoA_dh_1, 1 hit PF02770, Acyl-CoA_dh_M, 1 hit PF02771, Acyl-CoA_dh_N, 1 hit |
SUPFAMi | SSF47203, SSF47203, 1 hit SSF56645, SSF56645, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CHSE2_MYCTU | |
Accessioni | P71858Primary (citable) accession number: P71858 Secondary accession number(s): F2GEQ3, I6X7L6, O08027 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 30, 2016 |
Last sequence update: | July 1, 1997 | |
Last modified: | December 2, 2020 | |
This is version 136 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families