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Protein

Long-chain-fatty-acid--CoA ligase FadD15

Gene

fadD15

Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Status
Reviewed-Annotation score: -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.By similarity

Catalytic activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processFatty acid metabolism, Lipid metabolism
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00094

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain-fatty-acid--CoA ligase FadD15 (EC:6.2.1.3)
Short name:
FACL
Alternative name(s):
Acyl-CoA synthetase
Gene namesi
Name:fadD15
Ordered Locus Names:MMAR_3231
OrganismiMycobacterium marinum (strain ATCC BAA-535 / M)
Taxonomic identifieri216594 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000001190 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004067861 – 600Long-chain-fatty-acid--CoA ligase FadD15Add BLAST600

Interactioni

Protein-protein interaction databases

STRINGi216594.MMAR_3231

Structurei

3D structure databases

ProteinModelPortaliB2HGV4
SMRiB2HGV4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108IQE Bacteria
COG1022 LUCA
HOGENOMiHOG000229985
KOiK01897
OMAiSVLPIWH
OrthoDBiPOG091H032B

Family and domain databases

InterProiView protein in InterPro
IPR020845 AMP-binding_CS
IPR000873 AMP-dep_Synth/Lig
PfamiView protein in Pfam
PF00501 AMP-binding, 1 hit
PROSITEiView protein in PROSITE
PS00455 AMP_BINDING, 1 hit

Sequencei

Sequence statusi: Complete.

B2HGV4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRQYSVPARF SVDERDNVAA MVFEHERDDP DHIIYQRQID GIWTDITCAE
60 70 80 90 100
AARHIRSAAL GLIALGVQAG DRVSIFSATC YEWAILDLAI LAVGAVTVPI
110 120 130 140 150
YETSSAEQVR WVLQNSEAVL AFAETDAHAA MIAELTGDLP ALRRVLVING
160 170 180 190 200
SGPKALEQLA EEGGSVDRAE LTARLDALRS SDPATLIYTS GTTGRPKGCQ
210 220 230 240 250
LTHSNLLHEI RGTQECLPTL LTPGQRLLVF LPLAHVLARA LTLSAFASKV
260 270 280 290 300
TVGFTSDIKN LLPLFAVFKP TVVVSVPRVF EKVYNTAEQN ASNDGKGAIF
310 320 330 340 350
KLAAQTAVDW SRAWDDGRPG LLLRAKHALF DRLVYHKLRA ALGGDCHAAV
360 370 380 390 400
SGGAPLGARL GHFYRGVGLT IYEGYGLTET SAAVTVNQID ALKIGTVGKL
410 420 430 440 450
VPGNSLRIAD DGELLVRGGV VFSGYWRNEQ ATDEAFTDGW FRTGDLGAID
460 470 480 490 500
DDGFLSITGR KKELIVTAGG KNVAPAVLED QLRAHPLISQ AMVVGDAKPF
510 520 530 540 550
IGALITIDPE AFGGWKQRNS KADHAAVRDL AEDPDLVAEV DAAVKEANLA
560 570 580 590 600
VSHAESIRKF RILHVDFTED TGELTPTMKV KRNVVAEKFS VEIEAIYTKD
Length:600
Mass (Da):64,751
Last modified:June 10, 2008 - v1
Checksum:iCB132BBBF2E36150
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA Translation: ACC41657.1
RefSeqiWP_012394891.1, NC_010612.1

Genome annotation databases

EnsemblBacteriaiACC41657; ACC41657; MMAR_3231
KEGGimmi:MMAR_3231

Similar proteinsi

Entry informationi

Entry nameiFAC15_MYCMM
AccessioniPrimary (citable) accession number: B2HGV4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: June 10, 2008
Last modified: April 25, 2018
This is version 53 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health