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Protein

Gamma-butyrobetaine dioxygenase

Gene

BBOX1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Protein has several cofactor binding sites:

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

  • gamma-butyrobetaine dioxygenase activity Source: UniProtKB
  • iron ion binding Source: InterPro
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Carnitine biosynthesis

Keywords - Ligandi

Iron, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS05246-MONOMER.
BRENDAi1.14.11.1. 2681.
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 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:964. BBOX1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25274.

Chemistry

DrugBankiDB00139. Succinic acid.
DB00126. Vitamin C.

Polymorphism and mutation databases

BioMutaiBBOX1.

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

BgeeiO75936.
CleanExiHS_BBOX1.
ExpressionAtlasiO75936. baseline and differential.
GenevestigatoriO75936.

Organism-specific databases

HPAiHPA007600.
HPA027823.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
KIAA1598A0MZ66-73EBI-715662,EBI-10171490

Protein-protein interaction databases

BioGridi114008. 17 interactions.
IntActiO75936. 2 interactions.
MINTiMINT-1404070.
STRINGi9606.ENSP00000263182.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4CWDX-ray1.90A1-387[»]
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.
GeneTreeiENSGT00530000063582.
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

        10         20         30         40         50
MACTIQKAEA LDGAHLMQIL WYDEEESLYP AVWLRDNCPC SDCYLDSAKA
60 70 80 90 100
RKLLVEALDV NIGIKGLIFD RKKVYITWPD EHYSEFQADW LKKRCFSKQA
110 120 130 140 150
RAKLQRELFF PECQYWGSEL QLPTLDFEDV LRYDEHAYKW LSTLKKVGIV
160 170 180 190 200
RLTGASDKPG EVSKLGKRMG FLYLTFYGHT WQVQDKIDAN NVAYTTGKLS
210 220 230 240 250
FHTDYPALHH PPGVQLLHCI KQTVTGGDSE IVDGFNVCQK LKKNNPQAFQ
260 270 280 290 300
ILSSTFVDFT DIGVDYCDFS VQSKHKIIEL DDKGQVVRIN FNNATRDTIF
310 320 330 340 350
DVPVERVQPF YAALKEFVDL MNSKESKFTF KMNPGDVITF DNWRLLHGRR
360 370 380
SYEAGTEISR HLEGAYADWD VVMSRLRILR QRVENGN
Length:387
Mass (Da):44,715
Last modified:November 1, 1998 - v1
Checksum:iA3BA3F9FA9355DB3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
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:
EMBLi
GenBanki
DDBJi
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.
UniGeneiHs.591996.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4CWDX-ray1.90A1-387[»]
ProteinModelPortaliO75936.
SMRiO75936. Positions 1-384.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114008. 17 interactions.
IntActiO75936. 2 interactions.
MINTiMINT-1404070.
STRINGi9606.ENSP00000263182.

Chemistry

BindingDBiO75936.
ChEMBLiCHEMBL2163175.
DrugBankiDB00139. Succinic acid.
DB00126. Vitamin C.

PTM databases

PhosphoSiteiO75936.

Polymorphism and mutation databases

BioMutaiBBOX1.

Proteomic databases

PaxDbiO75936.
PRIDEiO75936.

Protocols and materials databases

DNASUi8424.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8424.
GeneCardsiGC11P027019.
HGNCiHGNC:964. BBOX1.
HPAiHPA007600.
HPA027823.
MIMi603312. gene.
neXtProtiNX_O75936.
PharmGKBiPA25274.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2175.
GeneTreeiENSGT00530000063582.
HOGENOMiHOG000231427.
HOVERGENiHBG031125.
InParanoidiO75936.
KOiK00471.
OMAiCAIQKAE.
OrthoDBiEOG7XPZ5P.
PhylomeDBiO75936.
TreeFamiTF313805.

Enzyme and pathway databases

UniPathwayiUPA00118.
BioCyciMetaCyc:HS05246-MONOMER.
BRENDAi1.14.11.1. 2681.
ReactomeiREACT_2125. Carnitine synthesis.
SABIO-RKO75936.

Miscellaneous databases

ChiTaRSiBBOX1. human.
EvolutionaryTraceiO75936.
GeneWikiiGamma-butyrobetaine_dioxygenase.
GenomeRNAii8424.
NextBioi31520.
PROiO75936.
SOURCEiSearch...

Gene expression databases

BgeeiO75936.
CleanExiHS_BBOX1.
ExpressionAtlasiO75936. baseline and differential.
GenevestigatoriO75936.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: May 27, 2015
This is version 131 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

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 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.