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Protein

Long-chain-fatty-acid--CoA/3-oxocholest-4-en-26-oate--CoA ligase

Gene

fadD19

Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the activation of long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension. Also involved in the degradation of cholesterol via the degradation of the side chains of C-24 branched-chain sterols. Catalyzes the ATP-dependent CoA thioesterification of the sterol 3-oxocholest-4-en-26-oate to yield 3-oxocholest-4-en-26-oyl-CoA.By similarity

Catalytic activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.By similarity
ATP + (25S)-3-oxocholest-4-en-26-oate + CoA = AMP + diphosphate + (25S)-3-oxocholest-4-en-26-oyl-CoA.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei419 – 4191ATPBy similarity
Binding sitei434 – 4341ATPBy similarity
Binding sitei525 – 5251ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi178 – 1869ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. long-chain fatty acid-CoA ligase activity Source: UniProtKB-EC

GO - Biological processi

  1. cholesterol metabolic process Source: UniProtKB-UniPathway
  2. fatty acid biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cholesterol metabolism, Fatty acid metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMMAR216594:GJOB-5043-MONOMER.
UniPathwayiUPA00094.
UPA00296.

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain-fatty-acid--CoA/3-oxocholest-4-en-26-oate--CoA ligaseBy similarity (EC:6.2.1.3By similarity, EC:6.2.1.42By similarity)
Short name:
FACLBy similarity
Alternative name(s):
Acyl-CoA synthetaseBy similarity
Steroid-CoA ligaseBy similarity
Steroid-coenzyme A ligaseBy similarity
Gene namesi
Name:fadD19By similarity
Synonyms:fadD19_1
Ordered Locus Names:MMAR_5001
OrganismiMycobacterium marinum (strain ATCC BAA-535 / M)
Taxonomic identifieri216594 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000001190 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 550550Long-chain-fatty-acid--CoA/3-oxocholest-4-en-26-oate--CoA ligasePRO_0000406792Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi216594.MMAR_5001.

Structurei

3D structure databases

ProteinModelPortaliB2HI05.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0318.
HOGENOMiHOG000230015.
KOiK18688.
OMAiMIHGGSQ.
OrthoDBiEOG6MSRZN.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2HI05-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVALNIADL AEHAIDAVPD RVALICGDEQ LTYAQLEEKA NRLAHHLIDQ
60 70 80 90 100
GVGKGDKVGL YCRNRIEIVI AMLGIIKAGA ILINVNFRYV EGELKYLFDN
110 120 130 140 150
SDMVALVHER QYADRVANVL PDTPNVKTIL VVQDGSDKDY RRYGGVEFYS
160 170 180 190 200
AIADSSPERD FAELQRERSA DDIYILYTGG TTGFPKGVMW RHEDIYRVLF
210 220 230 240 250
GGTDFATGEF IKDEYDLAKA AAANPPMIRY PIPPMIHGAT QSATWMSIFS
260 270 280 290 300
GQTTVLAPEF DADQVWRTIS DRKVNLLFFT GDAMARPLLD ALMKDNDYDL
310 320 330 340 350
SSLFLLASTA ALFSPSIKEK LLELLPNRVI TDSIGSSETG FGGTSIVGAG
360 370 380 390 400
QATTGGPRVT IDHRTVVLDE EGNEVKPGSG VRGIIAKKGN IPVGYYKDEK
410 420 430 440 450
KTAETFKTIN GVRYAIPGDY AMVEADGTVT MLGRGSVSIN SGGEKIYPEE
460 470 480 490 500
VEAALKGHPD VFDALVVGVP DPRYGQHVAA VVAPRPGSRP SLAELDGFVR
510 520 530 540 550
SAIAGYKVPR SLWFVDEVKR SPAGKPDYRW AKEQTEARPA DDVHAAHVSA
Length:550
Mass (Da):59,946
Last modified:June 10, 2008 - v1
Checksum:i6BA317E6E7E31ACB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC43405.1.
RefSeqiYP_001853260.1. NC_010612.1.

Genome annotation databases

EnsemblBacteriaiACC43405; ACC43405; MMAR_5001.
KEGGimmi:MMAR_5001.
PATRICi18071407. VBIMycMar75906_5360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC43405.1.
RefSeqiYP_001853260.1. NC_010612.1.

3D structure databases

ProteinModelPortaliB2HI05.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi216594.MMAR_5001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACC43405; ACC43405; MMAR_5001.
KEGGimmi:MMAR_5001.
PATRICi18071407. VBIMycMar75906_5360.

Phylogenomic databases

eggNOGiCOG0318.
HOGENOMiHOG000230015.
KOiK18688.
OMAiMIHGGSQ.
OrthoDBiEOG6MSRZN.

Enzyme and pathway databases

UniPathwayiUPA00094.
UPA00296.
BioCyciMMAR216594:GJOB-5043-MONOMER.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-535 / M.

Entry informationi

Entry nameiFAC19_MYCMM
AccessioniPrimary (citable) accession number: B2HI05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: June 10, 2008
Last modified: April 29, 2015
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.