Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Choline dehydrogenase, mitochondrial

Gene

Chdh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Choline + acceptor = betaine aldehyde + reduced acceptor.

Cofactori

FADBy similarity

Pathwayi: betaine biosynthesis via choline pathway

This protein is involved in step 1 of the subpathway that synthesizes betaine aldehyde from choline (cytochrome c reductase route).
Proteins known to be involved in this subpathway in this organism are:
  1. Choline dehydrogenase, mitochondrial (Chdh)
This subpathway is part of the pathway betaine biosynthesis via choline pathway, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes betaine aldehyde from choline (cytochrome c reductase route), the pathway betaine biosynthesis via choline pathway and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei516 – 5161Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi47 – 7933FADBy similarityAdd
BLAST

GO - Molecular functioni

  • choline dehydrogenase activity Source: RGD
  • flavin adenine dinucleotide binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.1.99.1. 5301.
ReactomeiR-RNO-6798163. Choline catabolism.
UniPathwayiUPA00529; UER00385.

Names & Taxonomyi

Protein namesi
Recommended name:
Choline dehydrogenase, mitochondrial (EC:1.1.99.1)
Short name:
CDH
Short name:
CHD
Gene namesi
Name:Chdh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi735166. Chdh.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434Mitochondrion1 PublicationAdd
BLAST
Chaini35 – 599565Choline dehydrogenase, mitochondrialPRO_0000418439Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei441 – 4411N6-succinyllysineBy similarity
Modified residuei489 – 4891N6-acetyllysine; alternateBy similarity
Modified residuei489 – 4891N6-succinyllysine; alternateBy similarity
Modified residuei501 – 5011N6-acetyllysine; alternateBy similarity
Modified residuei501 – 5011N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ6UPE0.
PRIDEiQ6UPE0.

PTM databases

iPTMnetiQ6UPE0.

Expressioni

Gene expression databases

GenevisibleiQ6UPE0. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021407.

Structurei

3D structure databases

ProteinModelPortaliQ6UPE0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GMC oxidoreductase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1238. Eukaryota.
COG2303. LUCA.
GeneTreeiENSGT00530000063260.
HOGENOMiHOG000139600.
HOVERGENiHBG023639.
InParanoidiQ6UPE0.
KOiK00108.
OMAiMWCLLRG.
OrthoDBiEOG7DFXBR.
PhylomeDBiQ6UPE0.
TreeFamiTF313911.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000137. Alcohol_oxidase. 1 hit.
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q6UPE0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWQVLRSWSK RCLSPRGALA WAAQGQPRPP CSCAVASAAS GGKDEYTFIV
60 70 80 90 100
VGAGSAGCVL ANRLTEDPNH RVLLLEAGPK DLLMGSKRLQ WKIHMPAALV
110 120 130 140 150
ANLCDDKYNW YYHTEAQPGL DGRVLYWPRG RVWGGSSSLN AMVYIRGHAE
160 170 180 190 200
DYNRWHRQGA EGWDYAHCLP YFRKAQKHEL GANMYRGGDG PLHVSRGKTN
210 220 230 240 250
HPLHQAFLQA ARQAGYPFTE DMNGFQQEGF GWMDMTIHQG KRWSTASAYL
260 270 280 290 300
RPALSRPNLR AEVQTLVSRV LFEGTRAVGV EYIKDGQSHK AYVSREVILS
310 320 330 340 350
GGAINSPQLL MLSGVGNADD LKKLGIPVVC HLPGVGQNLQ DHLEIYIQHA
360 370 380 390 400
CTQPITLHSA QKPLRKVCIG LEWLWRFTGD GATAHLETGG FIRSRPGVPH
410 420 430 440 450
PDIQFHFLPS QVIDHGRKPT QQEAYQVHVG TMRATSVGWL KLRSTNPQDH
460 470 480 490 500
PMINPNYLST ETDVEDFRQC VKLTREIFAQ EAFAPFRGKE LQPGSHVQSD
510 520 530 540 550
KEIDAFVRAK ADSAYHPSCT CKMGQPSDPT AVVDQQTRVI GVENLRVIDA
560 570 580 590
SIMPSVVSGN LNAPTIMIAE KAADVIKGCP ALGDENVPVY KPQTLDTQR
Length:599
Mass (Da):66,389
Last modified:July 5, 2004 - v1
Checksum:i8ECDC1089B6236D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY365023 mRNA. Translation: AAQ67365.1.
CH474046 Genomic DNA. Translation: EDL89007.1.
BC085787 mRNA. Translation: AAH85787.1.
RefSeqiNP_942026.1. NM_198731.2.
XP_006252640.1. XM_006252578.2.
XP_006252641.1. XM_006252579.2.
XP_006252642.1. XM_006252580.2.
XP_008769206.1. XM_008770984.1.
XP_008769207.1. XM_008770985.1.
UniGeneiRn.22857.

Genome annotation databases

EnsembliENSRNOT00000021407; ENSRNOP00000021407; ENSRNOG00000015859.
GeneIDi290551.
KEGGirno:290551.
UCSCiRGD:735166. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY365023 mRNA. Translation: AAQ67365.1.
CH474046 Genomic DNA. Translation: EDL89007.1.
BC085787 mRNA. Translation: AAH85787.1.
RefSeqiNP_942026.1. NM_198731.2.
XP_006252640.1. XM_006252578.2.
XP_006252641.1. XM_006252579.2.
XP_006252642.1. XM_006252580.2.
XP_008769206.1. XM_008770984.1.
XP_008769207.1. XM_008770985.1.
UniGeneiRn.22857.

3D structure databases

ProteinModelPortaliQ6UPE0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021407.

PTM databases

iPTMnetiQ6UPE0.

Proteomic databases

PaxDbiQ6UPE0.
PRIDEiQ6UPE0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000021407; ENSRNOP00000021407; ENSRNOG00000015859.
GeneIDi290551.
KEGGirno:290551.
UCSCiRGD:735166. rat.

Organism-specific databases

CTDi55349.
RGDi735166. Chdh.

Phylogenomic databases

eggNOGiKOG1238. Eukaryota.
COG2303. LUCA.
GeneTreeiENSGT00530000063260.
HOGENOMiHOG000139600.
HOVERGENiHBG023639.
InParanoidiQ6UPE0.
KOiK00108.
OMAiMWCLLRG.
OrthoDBiEOG7DFXBR.
PhylomeDBiQ6UPE0.
TreeFamiTF313911.

Enzyme and pathway databases

UniPathwayiUPA00529; UER00385.
BRENDAi1.1.99.1. 5301.
ReactomeiR-RNO-6798163. Choline catabolism.

Miscellaneous databases

PROiQ6UPE0.

Gene expression databases

GenevisibleiQ6UPE0. RN.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR012132. GMC_OxRdtase.
IPR000172. GMC_OxRdtase_N.
IPR007867. GMC_OxRtase_C.
[Graphical view]
PfamiPF05199. GMC_oxred_C. 1 hit.
PF00732. GMC_oxred_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000137. Alcohol_oxidase. 1 hit.
SUPFAMiSSF51905. SSF51905. 2 hits.
PROSITEiPS00623. GMC_OXRED_1. 1 hit.
PS00624. GMC_OXRED_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Functional expression and processing of rat choline dehydrogenase precursor."
    Huang S., Lin Q.
    Biochem. Biophys. Res. Commun. 309:344-350(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-48, TRANSIT PEPTIDE CLEAVAGE SITE, SUBCELLULAR LOCATION.
    Strain: Sprague-Dawley.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  4. "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.

Entry informationi

Entry nameiCHDH_RAT
AccessioniPrimary (citable) accession number: Q6UPE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.