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Protein

3-oxoacyl-[acyl-carrier-protein] reductase FabG1

Gene

fabG1

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

Functioni

Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. MabA preferentially metabolizes long-chain substrates (C8-C20) and has a poor affinity for the C4 substrate.3 Publications

Catalytic activityi

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.1 Publication

Kineticsi

  1. KM=8.3 µM for beta-ketododecanoyl-CoA (at 25 degrees Celsius and at pH 7.0)1 Publication
  2. KM=41 µM for NADPH (at 25 degrees Celsius and at pH 7.0)1 Publication
  3. KM=70 µM for beta-ketooctanoyl-CoA (at 25 degrees Celsius and at pH 7.0)1 Publication
  4. KM=1530 µM for acetoacetyl-CoA (at 25 degrees Celsius and at pH 7.0)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.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei27NADP; via amide nitrogen1
    Binding sitei47NADP1
    Binding sitei88NADP; via amide nitrogen1
    Binding sitei140SubstrateBy similarity1
    Active sitei153Proton acceptorPROSITE-ProRule annotation1
    Binding sitei186NADP; via amide nitrogen and carbonyl oxygenBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi22 – 25NADP4
    Nucleotide bindingi61 – 62NADP2
    Nucleotide bindingi153 – 157NADPBy similarity5

    GO - Molecular functioni

    GO - Biological processi

    • mycolic acid biosynthetic process Source: MTBBASE
    • oxidation-reduction process Source: MTBBASE
    • short-chain fatty acid metabolic process Source: MTBBASE

    Keywordsi

    Molecular functionOxidoreductase
    Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
    LigandNADP

    Enzyme and pathway databases

    UniPathwayiUPA00094

    Chemistry databases

    SwissLipidsiSLP:000001159

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-oxoacyl-[acyl-carrier-protein] reductase FabG1 (EC:1.1.1.100)
    Alternative name(s):
    3-ketoacyl-acyl carrier protein reductase
    Beta-ketoacyl-ACP reductase
    Beta-ketoacyl-acyl carrier protein reductase
    Gene namesi
    Name:fabG1
    Synonyms:mabA
    Ordered Locus Names:Rv1483
    ORF Names:MTCY277.04
    OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    Taxonomic identifieri83332 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    Proteomesi
    • UP000001584 Componenti: Chromosome

    Organism-specific databases

    TubercuListiRv1483

    Subcellular locationi

    GO - Cellular componenti

    • plasma membrane Source: MTBBASE

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi60C → V: Displays a lower activity than the wild-type and a slightly decreased affinity for the cofactor. Totally inactive; when associated with A-139 and L-144. 2 Publications1
    Mutagenesisi139G → A: Complete protein inactivation and freezes the catalytic site into its closed form. Totally inactive; when associated with V-60 and L-144. 1 Publication1
    Mutagenesisi144S → L: Stabilizes the catalytic loop in its open active form. Totally inactive; when associated with V-60 and A-139. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00000546772 – 2473-oxoacyl-[acyl-carrier-protein] reductase FabG1Add BLAST246

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylthreonineCombined sources1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP9WGT3

    PTM databases

    iPTMnetiP9WGT3

    Interactioni

    Subunit structurei

    Homotetramer.3 Publications

    Protein-protein interaction databases

    STRINGi83332.Rv1483

    Structurei

    Secondary structure

    1247
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi17 – 20Combined sources4
    Turni21 – 24Combined sources4
    Helixi26 – 37Combined sources12
    Beta strandi41 – 49Combined sources9
    Beta strandi55 – 59Combined sources5
    Helixi65 – 79Combined sources15
    Beta strandi83 – 88Combined sources6
    Turni97 – 99Combined sources3
    Helixi102 – 112Combined sources11
    Helixi114 – 129Combined sources16
    Beta strandi133 – 138Combined sources6
    Helixi142 – 145Combined sources4
    Helixi151 – 171Combined sources21
    Helixi172 – 174Combined sources3
    Beta strandi176 – 183Combined sources8
    Helixi189 – 193Combined sources5
    Helixi196 – 202Combined sources7
    Helixi203 – 205Combined sources3
    Helixi214 – 225Combined sources12
    Helixi227 – 229Combined sources3
    Beta strandi236 – 240Combined sources5
    Turni241 – 244Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1UZLX-ray2.00A/B1-247[»]
    1UZMX-ray1.49A/B1-247[»]
    1UZNX-ray1.91A/B1-247[»]
    2NTNX-ray2.30A/B1-247[»]
    ProteinModelPortaliP9WGT3
    SMRiP9WGT3
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CHR Bacteria
    ENOG410XNW1 LUCA
    KOiK11610
    OMAiGSRNIRC
    PhylomeDBiP9WGT3

    Family and domain databases

    InterProiView protein in InterPro
    IPR036291 NAD(P)-bd_dom_sf
    IPR020904 Sc_DH/Rdtase_CS
    IPR002347 SDR_fam
    PRINTSiPR00081 GDHRDH
    PR00080 SDRFAMILY
    SUPFAMiSSF51735 SSF51735, 1 hit
    PROSITEiView protein in PROSITE
    PS00061 ADH_SHORT, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P9WGT3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTATATEGAK PPFVSRSVLV TGGNRGIGLA IAQRLAADGH KVAVTHRGSG
    60 70 80 90 100
    APKGLFGVEC DVTDSDAVDR AFTAVEEHQG PVEVLVSNAG LSADAFLMRM
    110 120 130 140 150
    TEEKFEKVIN ANLTGAFRVA QRASRSMQRN KFGRMIFIGS VSGSWGIGNQ
    160 170 180 190 200
    ANYAASKAGV IGMARSIARE LSKANVTANV VAPGYIDTDM TRALDERIQQ
    210 220 230 240
    GALQFIPAKR VGTPAEVAGV VSFLASEDAS YISGAVIPVD GGMGMGH
    Length:247
    Mass (Da):25,697
    Last modified:April 16, 2014 - v1
    Checksum:i70F6254B0FFFCD47
    GO

    Mass spectrometryi

    Molecular mass is 27729 Da from positions 2 - 247. Determined by ESI. Recombinant protein expressed in E.coli.1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U66801 Genomic DNA Translation: AAC69639.1
    AL123456 Genomic DNA Translation: CCP44243.1
    PIRiF70710
    RefSeqiNP_215999.1, NC_000962.3
    WP_003898892.1, NZ_KK339370.1

    Genome annotation databases

    EnsemblBacteriaiCCP44243; CCP44243; Rv1483
    GeneIDi886551
    KEGGimtu:Rv1483

    Similar proteinsi

    Entry informationi

    Entry nameiFABG_MYCTU
    AccessioniPrimary (citable) accession number: P9WGT3
    Secondary accession number(s): L0T9R6
    , P0A5Y4, P71764, Q48930
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
    Last sequence update: April 16, 2014
    Last modified: March 28, 2018
    This is version 28 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

    3D-structure, Complete proteome, Reference proteome

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