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A0R1H7

- A0R1H7_MYCS2

UniProt

A0R1H7 - A0R1H7_MYCS2

Protein
Submitted name:

Fatty acid synthase

Gene

MSMEG_4757

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (09 Jan 2007)
      Previous versions | rss
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    Functioni

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei523 – 5231FMNImported
    Binding sitei550 – 5501FMNImported
    Binding sitei577 – 5771FMNImported
    Binding sitei582 – 5821FMNImported
    Binding sitei614 – 6141FMN; via amide nitrogenImported
    Binding sitei647 – 6471FMNImported

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi434 – 4363FMNImported

    GO - Molecular functioni

    1. enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: InterPro
    2. nucleotide binding Source: UniProtKB-KW

    GO - Biological processi

    1. fatty acid biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    TransferaseUniRule annotation

    Keywords - Ligandi

    Flavoprotein, FMNImported, Nucleotide-bindingImported

    Enzyme and pathway databases

    BioCyciMSME246196:GJ4Y-4756-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Fatty acid synthaseImported
    Gene namesi
    Ordered Locus Names:MSMEG_4757Imported, MSMEI_4637Imported
    OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)Imported
    Taxonomic identifieri246196 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000000757: Chromosome, UP000006158: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. fatty acid synthase complex Source: InterPro

    Interactioni

    Protein-protein interaction databases

    STRINGi246196.MSMEG_4757.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZENelectron microscopy7.50D/E/F1-3089[»]
    4B3Yelectron microscopy7.50A/B/C1-3089[»]
    4BJDelectron microscopy20.00A/B/C1-3089[»]
    4BJEelectron microscopy20.00D/E/F1-3089[»]
    4BJFelectron microscopy17.50D/E/F1-3089[»]
    4BJGelectron microscopy17.50A/B/C1-3089[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    eggNOGiCOG4982.
    HOGENOMiHOG000051526.
    KOiK11533.
    OMAiMFLDPYL.
    OrthoDBiEOG6WMHTT.

    Family and domain databases

    Gene3Di3.10.129.10. 1 hit.
    3.20.20.70. 1 hit.
    3.40.366.10. 5 hits.
    3.40.47.10. 3 hits.
    3.40.50.720. 1 hit.
    InterProiIPR001227. Ac_transferase_dom.
    IPR014043. Acyl_transferase.
    IPR016035. Acyl_Trfase/lysoPLipase.
    IPR013785. Aldolase_TIM.
    IPR013565. DUF1729.
    IPR003965. Fatty_acid_synthase.
    IPR029069. HotDog_dom.
    IPR014031. Ketoacyl_synth_C.
    IPR014030. Ketoacyl_synth_N.
    IPR002539. MaoC_dom.
    IPR016040. NAD(P)-bd_dom.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view]
    PfamiPF00698. Acyl_transf_1. 2 hits.
    PF08354. DUF1729. 1 hit.
    PF00109. ketoacyl-synt. 1 hit.
    PF02801. Ketoacyl-synt_C. 1 hit.
    PF01575. MaoC_dehydratas. 1 hit.
    [Graphical view]
    PRINTSiPR01483. FASYNTHASE.
    SUPFAMiSSF52151. SSF52151. 5 hits.
    SSF53901. SSF53901. 2 hits.
    SSF54637. SSF54637. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A0R1H7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTIYEHDRVP AGWNDESGSD RTADGNAADT AHALVDRLSA GEPYAVAFGG     50
    QGSAWLETLE ELVSSAGIES ELATLAGEAE LLLEPVASEL VVVRPIGFEP 100
    LQWVRALAAE EPVPSDKQLT SAAVSVPGVL LTQIAAVRAL ARQGMDLTAT 150
    PPVAVAGHSQ GVLAVQALAA KGAKDVELLA LAQLIGAAGT LVARRRGITV 200
    LGDRPPMVSV TNADPERIYE LLEEFSSDVR TVLPPVLSIR NGRRSVVITG 250
    TPEQLSRFEL YCTQIAEKEE AERKNKLRGG AVFAPVFDPV QVEVGFHTPR 300
    LSDGIEIVGR WAETVGLDVE LAKELTESIL VRQVDWVDEI TELHEAGARW 350
    ILDLGPGDIL TRLTAPVIRG LGIGIVPAAT RGGQRNLFTV GAVPEVARPW 400
    SSYAPTVVKL PDGSVKLETK FTRLTGRSPI LLAGMTPTTV DAKIVAAAAN 450
    AGHWAELAGG GQVTEQIFND RIAELETLLE PGRAIQFNTL FLDPYLWKLQ 500
    VGGKRLVQRA RQSGAPIDGL VVSAGIPDLE EAVDIIDELN EVGISHVVFK 550
    PGTVEQIRSV IRIAAEVPTK PVIVHIEGGR AGGHHSWEDL DDLLLATYSE 600
    LRSRSNITIC VGGGIGTPER SAEYLSGRWA EVHGYPLMPI DGILVGTAAM 650
    ATLEATTSPQ VKQLLVETKG TEAWVGAGKA ANGMASGRSQ LGADIHEIDN 700
    AASRCGRLLD EVAGDADAVA ERRDEIIAAM AQTAKPYFGD VAEMTYLQWL 750
    RRYVELAIGD GNSTADTKRP DSPWLDITWR DRFEQMLKRA EARLHPQDFG 800
    PIETLFDADA DGERLLEDPE AAITALLQRY PDAETVVLHP ADVPFFVELC 850
    KTLGKPVNFV PVIDKDVRRW WRSDSLWQAH DARYEADQVC VIPGTAAVAG 900
    ITRVDEPVGE LLDRFEQAAV DEVLGAGAEP VEVLSRRQAR RDASGPLAVV 950
    LDAPDVLWAG RMSVNPVHRI AAPTEWQVRE GSDNRSASHP STGARLEVAD 1000
    DQHVVLSVPL SGTWIEIRFT LTDVVRSGGA PIVEVDDAAT AMRAVLAIAA 1050
    GVEGPENLPK VVDNTATVTV DWDPERVADH TGVTATFGAP LAPTLTVVPD 1100
    ALVGRCWPAV FAAIGSAATE AGFPVIEGLL SLVHLDHAAR LLAELPKEPA 1150
    EFTVTAKASA ATDTEVGRVV PVSVEVRNAA DGALLATLEE RFAIRGRTGA 1200
    AELTDPVRAG GAISDNATDT PRRRRRDVTV GAPVDMRPFA VVSGDHNPIH 1250
    TDRAAALLAG LEGPIVHGMW LSAAAQHVVT ATDGKPVPPA KLIGWTARFL 1300
    GMVKPGDQVD FRVDRVGIDV GAEVLEVSAR IGSELVMAAT ARLAAPKTVY 1350
    AFPGQGIQHK GMGMEVRARS KAARKVWDSA DKFTRETLGF SVLHVVRDNP 1400
    TSLIASGVHY HHPDGVLFLT QFTQVAMATV AAAQVAEMRE QGAFVEGAIA 1450
    CGHSVGEYTA LACVSGVYEL EALLEVVFHR GSKMHDIVPR DELGRSNYRL 1500
    AAIRPSQIDL DDADVKDFVA EISERTGEFL EIVNFNLRGS QYAIAGTVAG 1550
    LEALEEEIER RRQITGGKRS FILVPGIDVP FHSSVLRVGV ADFRRSLERV 1600
    MPRDKDPELI IGRYIPNLVP RPFTLDRDFI QEIRDLVPAE PLDEVLADYD 1650
    TWRNEKPKEL CRKVVIELLA WQFASPVRWI ETQDLLFIEE AAGGLGVERF 1700
    VEIGVKSAPT VAGLATNTLK LPEYSHSTVE VLNSERDAAV LFATDTDPEP 1750
    EPEADEPTAD APAEAAPAAA AAPAPVAAPA APSGGPRPDD ITFDAADATV 1800
    ALIALSAKMR IDQIEALDSI ESITDGASSR RNQLLVDLGS ELNLGAIDGA 1850
    AEADLGALKG QVTKLARTYK PFGPVLSDAI NDQLRTVLGP SGKRPAYITE 1900
    RVTKTWELGP GWAKHVTVEF ALGTREGSSV RGGDLGGLHA GALASAADVD 1950
    KVIDGAVAAV AARRGISVSL PSAGGASGGV VDSAALGEFA EKVTGPDGVL 2000
    ASAARLVLNQ LGLSDVVTTP EAATDAELID LVTAELGSDW PRLVAPTFDA 2050
    RKAVVFDDRW ASAREDLVKL WLAEEGDIDA QWEQLSQRFE GTGHVVATQA 2100
    NWWQGKALAA GRNVHASLFG RIAAGAENPG KGRYSDEVAV VTGASKGSIA 2150
    ASVVGQLLDG GATVIATTSR LDDDRLAFYK QLYRDHARFD ATLWVVPANM 2200
    ASYSDIDKLV EWVGTEQTES LGPQSIHLKD AQTPTLLFPF AAPRVAGDMS 2250
    EVGSRAEMEM KVLLWAVQRL ISGLSKIGAE RDIASRLHVV LPGSPNRGMF 2300
    GGDGAYGEAK SALDALENRW SAEKSWAERV SLAHALIGWT KGTGLMGQND 2350
    AIVSAVEEAG VTTYTTDEMA AMLLDLCTVE TKVAAAGAPV KVDLTGGLGD 2400
    IKIDMAELAA KAREEMSGAA DESDDEAPAG TIRALPSPPR GYNPAPAPEW 2450
    DDLDVDPADL VVIVGGAELG PYGSSRTRFE MEVSGELSAA GVLELAWTTG 2500
    MVKWEDDPKA GWYDTETGEL VPECEIVERY HDAVVERCGI REFVDDGAID 2550
    PDHASPLLVS VFLDKDFTFV VSSEADARAF VQFDPEHTVA RPLPDSSDWE 2600
    VTRKAGTEIR VPRKTKLSRT VGAQIPTGFD PTVWGISPDM ASSIDRVALW 2650
    NIVATVDAFL SSGFTPTELM RWVHPSQVAS TQGTGMGGMT SMQTMYHGNL 2700
    LGRAKPNDIL QEVLPNVVAA HVMQSYVGGY GAMVHPVGAC ATAAVSVEEG 2750
    VDKIKLGKAD LVIAGGFDDL TLEAIIGFGD MAATADTEMM RAKGISDSKF 2800
    SRANDRRRLG FLEAQGGGTI LLARGDLALK MGLPVLAVVG YAQSFADGVH 2850
    TSIPAPGLGA LGAARGGRES TLARSLAQLG VGADDIAVIS KHDTSTLAND 2900
    PNETELHERI ADSMGRAPGN PLFIVSQKTL TGHAKGGAAV FQMMGLCQIL 2950
    RDGVIPPNRS LDCVDDELAT SGHFVWVREP LDLRGKFPLK AGLVTSLGFG 3000
    HVSGLVALVH PEAFIAALDP SEREDYRTRA EQRMLAGQRR LVSAIAGGRP 3050
    MYEKPADRRF DHDVPEKRQE AAMLLSTDAR LGENDQYVL 3089
    Length:3,089
    Mass (Da):329,538
    Last modified:January 9, 2007 - v1
    Checksum:i251351CB2F8E7CF1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000480 Genomic DNA. Translation: ABK70103.1.
    CP001663 Genomic DNA. Translation: AFP41086.1.
    RefSeqiYP_006569381.1. NC_018289.1.
    YP_889015.1. NC_008596.1.

    Genome annotation databases

    EnsemblBacteriaiABK70103; ABK70103; MSMEG_4757.
    AFP41086; AFP41086; MSMEI_4637.
    GeneIDi4532653.
    KEGGimsg:MSMEI_4637.
    msm:MSMEG_4757.
    PATRICi18081817. VBIMycSme59918_4642.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000480 Genomic DNA. Translation: ABK70103.1 .
    CP001663 Genomic DNA. Translation: AFP41086.1 .
    RefSeqi YP_006569381.1. NC_018289.1.
    YP_889015.1. NC_008596.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ZEN electron microscopy 7.50 D/E/F 1-3089 [» ]
    4B3Y electron microscopy 7.50 A/B/C 1-3089 [» ]
    4BJD electron microscopy 20.00 A/B/C 1-3089 [» ]
    4BJE electron microscopy 20.00 D/E/F 1-3089 [» ]
    4BJF electron microscopy 17.50 D/E/F 1-3089 [» ]
    4BJG electron microscopy 17.50 A/B/C 1-3089 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 246196.MSMEG_4757.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABK70103 ; ABK70103 ; MSMEG_4757 .
    AFP41086 ; AFP41086 ; MSMEI_4637 .
    GeneIDi 4532653.
    KEGGi msg:MSMEI_4637.
    msm:MSMEG_4757.
    PATRICi 18081817. VBIMycSme59918_4642.

    Phylogenomic databases

    eggNOGi COG4982.
    HOGENOMi HOG000051526.
    KOi K11533.
    OMAi MFLDPYL.
    OrthoDBi EOG6WMHTT.

    Enzyme and pathway databases

    BioCyci MSME246196:GJ4Y-4756-MONOMER.

    Family and domain databases

    Gene3Di 3.10.129.10. 1 hit.
    3.20.20.70. 1 hit.
    3.40.366.10. 5 hits.
    3.40.47.10. 3 hits.
    3.40.50.720. 1 hit.
    InterProi IPR001227. Ac_transferase_dom.
    IPR014043. Acyl_transferase.
    IPR016035. Acyl_Trfase/lysoPLipase.
    IPR013785. Aldolase_TIM.
    IPR013565. DUF1729.
    IPR003965. Fatty_acid_synthase.
    IPR029069. HotDog_dom.
    IPR014031. Ketoacyl_synth_C.
    IPR014030. Ketoacyl_synth_N.
    IPR002539. MaoC_dom.
    IPR016040. NAD(P)-bd_dom.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view ]
    Pfami PF00698. Acyl_transf_1. 2 hits.
    PF08354. DUF1729. 1 hit.
    PF00109. ketoacyl-synt. 1 hit.
    PF02801. Ketoacyl-synt_C. 1 hit.
    PF01575. MaoC_dehydratas. 1 hit.
    [Graphical view ]
    PRINTSi PR01483. FASYNTHASE.
    SUPFAMi SSF52151. SSF52151. 5 hits.
    SSF53901. SSF53901. 2 hits.
    SSF54637. SSF54637. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE.
      Strain: MC2 155Imported.
    2. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
      Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155 and MC2 155Imported.
    3. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
      Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
      Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155Imported and MC2 155Imported.
    4. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
      Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
      Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700084 / mc(2)155 and MC2 155.
    5. "7.5-A cryo-em structure of the mycobacterial fatty acid synthase."
      Boehringer D., Ban N., Leibundgut M.
      J. Mol. Biol. 425:841-849(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.50 ANGSTROMS) IN COMPLEX WITH FMN.
    6. "Structure and conformational variability of the mycobacterium tuberculosis fatty acid synthase multienzyme complex."
      Ciccarelli L., Connell S.R., Enderle M., Mills D.J., Vonck J., Grininger M.
      Structure 21:1251-1257(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (17.50 ANGSTROMS) IN COMPLEX WITH FMN.

    Entry informationi

    Entry nameiA0R1H7_MYCS2
    AccessioniPrimary (citable) accession number: A0R1H7
    Entry historyi
    Integrated into UniProtKB/TrEMBL: January 9, 2007
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 67 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported, Complete proteome, Reference proteomeImported

    External Data

    Dasty 3