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O75936

- BODG_HUMAN

UniProt

O75936 - BODG_HUMAN

Protein

Gamma-butyrobetaine dioxygenase

Gene

BBOX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Catalyzes the formation of L-carnitine from gamma-butyrobetaine.

    Catalytic activityi

    4-trimethylammoniobutanoate + 2-oxoglutarate + O2 = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2.1 Publication

    Cofactori

    Binds 1 Fe2+ ion per subunit.Curated
    Ascorbate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi38 – 381Zinc
    Metal bindingi40 – 401Zinc
    Metal bindingi43 – 431Zinc
    Metal bindingi82 – 821Zinc
    Metal bindingi202 – 2021Iron; catalyticCurated
    Metal bindingi204 – 2041Iron; catalyticCurated
    Metal bindingi347 – 3471Iron; catalyticCurated

    GO - Molecular functioni

    1. gamma-butyrobetaine dioxygenase activity Source: UniProtKB
    2. iron ion binding Source: InterPro
    3. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. carnitine biosynthetic process Source: UniProtKB
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Carnitine biosynthesis

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05246-MONOMER.
    ReactomeiREACT_2125. Carnitine synthesis.
    SABIO-RKO75936.
    UniPathwayiUPA00118.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gamma-butyrobetaine dioxygenase (EC:1.14.11.1)
    Alternative name(s):
    Gamma-butyrobetaine hydroxylase
    Short name:
    Gamma-BBH
    Gamma-butyrobetaine,2-oxoglutarate dioxygenase
    Gene namesi
    Name:BBOX1
    Synonyms:BBH, BBOX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:964. BBOX1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrion Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25274.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 387387Gamma-butyrobetaine dioxygenasePRO_0000207085Add
    BLAST

    Proteomic databases

    PaxDbiO75936.
    PRIDEiO75936.

    PTM databases

    PhosphoSiteiO75936.

    Expressioni

    Tissue specificityi

    Highly expressed in kidney; moderately expressed in liver; very low expression in brain.

    Gene expression databases

    ArrayExpressiO75936.
    BgeeiO75936.
    CleanExiHS_BBOX1.
    GenevestigatoriO75936.

    Organism-specific databases

    HPAiHPA007600.
    HPA027823.

    Interactioni

    Protein-protein interaction databases

    BioGridi114008. 1 interaction.
    IntActiO75936. 1 interaction.
    MINTiMINT-1404070.
    STRINGi9606.ENSP00000263182.

    Structurei

    Secondary structure

    387
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni1 – 33
    Beta strandi4 – 118
    Turni12 – 154
    Beta strandi16 – 216
    Beta strandi26 – 305
    Helixi31 – 366
    Turni41 – 433
    Turni46 – 494
    Helixi55 – 573
    Beta strandi65 – 695
    Beta strandi71 – 777
    Beta strandi83 – 875
    Helixi88 – 936
    Helixi98 – 10912
    Beta strandi124 – 1263
    Helixi127 – 1326
    Helixi134 – 14714
    Beta strandi148 – 1536
    Beta strandi157 – 1593
    Helixi161 – 1699
    Beta strandi178 – 1847
    Helixi192 – 1943
    Beta strandi195 – 1973
    Beta strandi199 – 2024
    Beta strandi208 – 2103
    Beta strandi213 – 2219
    Beta strandi224 – 2263
    Beta strandi229 – 2335
    Helixi234 – 24411
    Helixi246 – 2527
    Beta strandi256 – 28025
    Beta strandi286 – 2894
    Turni293 – 2953
    Helixi304 – 3063
    Helixi307 – 32216
    Turni324 – 3263
    Beta strandi328 – 3303
    Beta strandi337 – 3415
    Turni342 – 3443
    Beta strandi345 – 3495
    Beta strandi361 – 3677
    Helixi369 – 38315

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MS5X-ray1.82A1-387[»]
    3N6WX-ray2.00A1-387[»]
    3O2GX-ray1.78A1-387[»]
    4BG1X-ray1.89A1-387[»]
    4BGKX-ray2.18A1-387[»]
    4BGMX-ray2.40A1-387[»]
    4BHFX-ray2.05A1-387[»]
    4BHGX-ray1.85A1-387[»]
    4BHIX-ray2.15A1-387[»]
    4C5WX-ray1.70A1-387[»]
    4C8RX-ray2.82A/B/C/D/E/F1-387[»]
    ProteinModelPortaliO75936.
    SMRiO75936. Positions 1-384.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75936.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the gamma-BBH/TMLD family.Curated

    Phylogenomic databases

    eggNOGiCOG2175.
    HOGENOMiHOG000231427.
    HOVERGENiHBG031125.
    InParanoidiO75936.
    KOiK00471.
    OMAiCAIQKAE.
    OrthoDBiEOG7XPZ5P.
    PhylomeDBiO75936.
    TreeFamiTF313805.

    Family and domain databases

    InterProiIPR012775. 2-oxoglut_dOase.
    IPR010376. DUF971.
    IPR003819. Taurine_dOase.
    [Graphical view]
    PfamiPF06155. DUF971. 1 hit.
    PF02668. TauD. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02409. carnitine_bodg. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O75936-1 [UniParc]FASTAAdd to Basket

    « Hide

    MACTIQKAEA LDGAHLMQIL WYDEEESLYP AVWLRDNCPC SDCYLDSAKA    50
    RKLLVEALDV NIGIKGLIFD RKKVYITWPD EHYSEFQADW LKKRCFSKQA 100
    RAKLQRELFF PECQYWGSEL QLPTLDFEDV LRYDEHAYKW LSTLKKVGIV 150
    RLTGASDKPG EVSKLGKRMG FLYLTFYGHT WQVQDKIDAN NVAYTTGKLS 200
    FHTDYPALHH PPGVQLLHCI KQTVTGGDSE IVDGFNVCQK LKKNNPQAFQ 250
    ILSSTFVDFT DIGVDYCDFS VQSKHKIIEL DDKGQVVRIN FNNATRDTIF 300
    DVPVERVQPF YAALKEFVDL MNSKESKFTF KMNPGDVITF DNWRLLHGRR 350
    SYEAGTEISR HLEGAYADWD VVMSRLRILR QRVENGN 387
    Length:387
    Mass (Da):44,715
    Last modified:November 1, 1998 - v1
    Checksum:iA3BA3F9FA9355DB3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF082868 mRNA. Translation: AAC64066.1.
    CR456812 mRNA. Translation: CAG33093.1.
    AK313422 mRNA. Translation: BAG36214.1.
    CH471064 Genomic DNA. Translation: EAW68290.1.
    CH471064 Genomic DNA. Translation: EAW68291.1.
    BC011034 mRNA. Translation: AAH11034.1.
    CCDSiCCDS7862.1.
    PIRiJE0360.
    RefSeqiNP_003977.1. NM_003986.2.
    XP_005253216.1. XM_005253159.2.
    XP_005253217.1. XM_005253160.2.
    XP_005253218.1. XM_005253161.2.
    XP_005253220.1. XM_005253163.2.
    XP_006718407.1. XM_006718344.1.
    UniGeneiHs.591996.

    Genome annotation databases

    EnsembliENST00000263182; ENSP00000263182; ENSG00000129151.
    ENST00000525090; ENSP00000433772; ENSG00000129151.
    ENST00000528583; ENSP00000434918; ENSG00000129151.
    ENST00000529202; ENSP00000435781; ENSG00000129151.
    GeneIDi8424.
    KEGGihsa:8424.
    UCSCiuc001mre.1. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF082868 mRNA. Translation: AAC64066.1 .
    CR456812 mRNA. Translation: CAG33093.1 .
    AK313422 mRNA. Translation: BAG36214.1 .
    CH471064 Genomic DNA. Translation: EAW68290.1 .
    CH471064 Genomic DNA. Translation: EAW68291.1 .
    BC011034 mRNA. Translation: AAH11034.1 .
    CCDSi CCDS7862.1.
    PIRi JE0360.
    RefSeqi NP_003977.1. NM_003986.2.
    XP_005253216.1. XM_005253159.2.
    XP_005253217.1. XM_005253160.2.
    XP_005253218.1. XM_005253161.2.
    XP_005253220.1. XM_005253163.2.
    XP_006718407.1. XM_006718344.1.
    UniGenei Hs.591996.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MS5 X-ray 1.82 A 1-387 [» ]
    3N6W X-ray 2.00 A 1-387 [» ]
    3O2G X-ray 1.78 A 1-387 [» ]
    4BG1 X-ray 1.89 A 1-387 [» ]
    4BGK X-ray 2.18 A 1-387 [» ]
    4BGM X-ray 2.40 A 1-387 [» ]
    4BHF X-ray 2.05 A 1-387 [» ]
    4BHG X-ray 1.85 A 1-387 [» ]
    4BHI X-ray 2.15 A 1-387 [» ]
    4C5W X-ray 1.70 A 1-387 [» ]
    4C8R X-ray 2.82 A/B/C/D/E/F 1-387 [» ]
    ProteinModelPortali O75936.
    SMRi O75936. Positions 1-384.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114008. 1 interaction.
    IntActi O75936. 1 interaction.
    MINTi MINT-1404070.
    STRINGi 9606.ENSP00000263182.

    Chemistry

    ChEMBLi CHEMBL2163175.
    DrugBanki DB00139. Succinic acid.
    DB00126. Vitamin C.

    PTM databases

    PhosphoSitei O75936.

    Proteomic databases

    PaxDbi O75936.
    PRIDEi O75936.

    Protocols and materials databases

    DNASUi 8424.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263182 ; ENSP00000263182 ; ENSG00000129151 .
    ENST00000525090 ; ENSP00000433772 ; ENSG00000129151 .
    ENST00000528583 ; ENSP00000434918 ; ENSG00000129151 .
    ENST00000529202 ; ENSP00000435781 ; ENSG00000129151 .
    GeneIDi 8424.
    KEGGi hsa:8424.
    UCSCi uc001mre.1. human.

    Organism-specific databases

    CTDi 8424.
    GeneCardsi GC11P027019.
    HGNCi HGNC:964. BBOX1.
    HPAi HPA007600.
    HPA027823.
    MIMi 603312. gene.
    neXtProti NX_O75936.
    PharmGKBi PA25274.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2175.
    HOGENOMi HOG000231427.
    HOVERGENi HBG031125.
    InParanoidi O75936.
    KOi K00471.
    OMAi CAIQKAE.
    OrthoDBi EOG7XPZ5P.
    PhylomeDBi O75936.
    TreeFami TF313805.

    Enzyme and pathway databases

    UniPathwayi UPA00118 .
    BioCyci MetaCyc:HS05246-MONOMER.
    Reactomei REACT_2125. Carnitine synthesis.
    SABIO-RK O75936.

    Miscellaneous databases

    EvolutionaryTracei O75936.
    GeneWikii Gamma-butyrobetaine_dioxygenase.
    GenomeRNAii 8424.
    NextBioi 31520.
    PROi O75936.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75936.
    Bgeei O75936.
    CleanExi HS_BBOX1.
    Genevestigatori O75936.

    Family and domain databases

    InterProi IPR012775. 2-oxoglut_dOase.
    IPR010376. DUF971.
    IPR003819. Taurine_dOase.
    [Graphical view ]
    Pfami PF06155. DUF971. 1 hit.
    PF02668. TauD. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02409. carnitine_bodg. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Carnitine biosynthesis: identification of the cDNA encoding human gamma-butyrobetaine hydroxylase."
      Vaz F.M., van Gool S., Ofman R., Ijlst L., Wanders R.J.A.
      Biochem. Biophys. Res. Commun. 250:506-510(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cerebellum.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.
    6. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS, CATALYTIC ACTIVITY, SUBUNIT.

    Entry informationi

    Entry nameiBODG_HUMAN
    AccessioniPrimary (citable) accession number: O75936
    Secondary accession number(s): B2R8L7, D3DQZ1, Q6IBJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 124 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3