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Protein

Long-chain-fatty-acid--AMP ligase FadD32

Gene

fadD32

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase (PKS) for further chain extension.1 Publication

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

  • adenylyltransferase activity Source: MTBBASE
  • ATP binding Source: UniProtKB-KW
  • ligase activity Source: UniProtKB

GO - Biological processi

  • Actinobacterium-type cell wall biogenesis Source: UniProtKB
  • fatty acid biosynthetic process Source: GO_Central
  • growth Source: MTBBASE
  • lipid biosynthetic process Source: UniProtKB
  • mycolate cell wall layer assembly Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:RV3801C-MONOMER.
MTBRV:RV3801C-MONOMER.
UniPathwayiUPA00094.

Chemistry

SwissLipidsiSLP:000000972.

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain-fatty-acid--AMP ligase FadD32 (EC:6.2.1.-)
Short name:
FAAL
Alternative name(s):
Acyl-AMP synthetase
Gene namesi
Name:fadD32
Ordered Locus Names:Rv3801c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3801c.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi383 – 3831F → A: Catalyzes the formation of acyl-CoA; when associated with A-481. 1 Publication
Mutagenesisi481 – 4811F → A: Catalyzes the formation of acyl-CoA; when associated with A-383. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637Long-chain-fatty-acid--AMP ligase FadD32PRO_0000406634Add
BLAST

Proteomic databases

PaxDbiO53580.
PRIDEiO53580.

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv3801c.

Structurei

3D structure databases

ProteinModelPortaliO53580.
SMRiO53580. Positions 25-623.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107RCI. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000266721.
InParanoidiO53580.
KOiK12428.
OMAiVDEWAVI.
PhylomeDBiO53580.

Family and domain databases

InterProiIPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O53580-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFVTGESGMA YHNPFIVNGK IRFPANTNLV RHVEKWAKVR GDKLAYRFLD
60 70 80 90 100
FSTERDGVAR DILWSDFSAR NRAVGARLQQ VTQPGDRVAI LCPQNLDYLI
110 120 130 140 150
SFFGALYSGR IAVPLFDPAE PGHVGRLHAV LDDCAPSTIL TTTDSAEGVR
160 170 180 190 200
KFIRARSAKE RPRVIAVDAV PTEVAATWQQ PEANEETVAY LQYTSGSTRI
210 220 230 240 250
PSGVQITHLN LPTNVVQVLN ALEGQEGDRG VSWLPFFHDM GLITVLLASV
260 270 280 290 300
LGHSFTFMTP AAFVRRPGRW IRELARKPGE TGGTFSAAPN FAFEHAAVRG
310 320 330 340 350
VPRDDEPPLD LSNVKGILNG SEPVSPASMR KFFEAFAPYG LKQTAVKPSY
360 370 380 390 400
GLAEATLFVS TTPMDEVPTV IHVDRDELNN QRFVEVAADA PNAVAQVSAG
410 420 430 440 450
KVGVSEWAVI VDADTASELP DGQIGEIWLH GNNLGTGYWG KEEESAQTFK
460 470 480 490 500
NILKSRISES RAEGAPDDAL WVRTGDYGTY FKDHLYIAGR IKDLVIIDGR
510 520 530 540 550
NHYPQDLECT AQESTKALRV GYAAAFSVPA NQLPQTVFDD SHAGLKFDPE
560 570 580 590 600
DTSEQLVIVG ERAAGTHKLD HQPIVDDIRA AIAVGHGVTV RDVLLVSAGT
610 620 630
IPRTSSGKIG RRACRAAYLD GSLRSGVGSP TVFATSD
Length:637
Mass (Da):69,232
Last modified:June 1, 1998 - v1
Checksum:i0A3A86CED9AE0EDC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46630.1.
PIRiE70887.
RefSeqiNP_218318.1. NC_000962.3.
WP_003899700.1. NC_000962.3.

Genome annotation databases

EnsemblBacteriaiCCP46630; CCP46630; Rv3801c.
GeneIDi886130.
KEGGimtu:Rv3801c.
mtv:RVBD_3801c.
PATRICi18157060. VBIMycTub87468_4232.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46630.1.
PIRiE70887.
RefSeqiNP_218318.1. NC_000962.3.
WP_003899700.1. NC_000962.3.

3D structure databases

ProteinModelPortaliO53580.
SMRiO53580. Positions 25-623.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3801c.

Chemistry

SwissLipidsiSLP:000000972.

Proteomic databases

PaxDbiO53580.
PRIDEiO53580.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP46630; CCP46630; Rv3801c.
GeneIDi886130.
KEGGimtu:Rv3801c.
mtv:RVBD_3801c.
PATRICi18157060. VBIMycTub87468_4232.

Organism-specific databases

TubercuListiRv3801c.

Phylogenomic databases

eggNOGiENOG4107RCI. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000266721.
InParanoidiO53580.
KOiK12428.
OMAiVDEWAVI.
PhylomeDBiO53580.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciMetaCyc:RV3801C-MONOMER.
MTBRV:RV3801C-MONOMER.

Family and domain databases

InterProiIPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFAA32_MYCTU
AccessioniPrimary (citable) accession number: O53580
Secondary accession number(s): L0TGT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: June 1, 1998
Last modified: September 7, 2016
This is version 93 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. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.