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Protein

Molybdenum cofactor synthesis protein cinnamon

Gene

cin

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.1 Publication

Catalytic activityi

ATP + molybdopterin = diphosphate + adenylyl-molybdopterin.
Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.

Cofactori

Mg2+By similarity

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. molybdopterin adenylyltransferase activity Source: GO_Central
  4. molybdopterin molybdotransferase activity Source: GO_Central

GO - Biological processi

  1. embryonic development via the syncytial blastoderm Source: FlyBase
  2. molybdenum incorporation into molybdenum-molybdopterin complex Source: GO_Central
  3. Mo-molybdopterin cofactor biosynthetic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Molybdenum, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_180227. Molybdenum cofactor biosynthesis.
UniPathwayiUPA00344.

Names & Taxonomyi

Protein namesi
Recommended name:
Molybdenum cofactor synthesis protein cinnamon
Including the following 2 domains:
Molybdopterin adenylyltransferase (EC:2.7.7.75)
Short name:
MPT adenylyltransferase
Alternative name(s):
Domain G
Molybdopterin molybdenumtransferase (EC:2.10.1.1)
Short name:
MPT Mo-transferase
Alternative name(s):
Domain E
Gene namesi
Name:cin
ORF Names:CG2945
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0000316. cin.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 601601Molybdenum cofactor synthesis protein cinnamonPRO_0000170962Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei376 – 3761Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP39205.

Expressioni

Developmental stagei

Detected primarily in the epidermal cells of the segmental grooves during germ-band retraction (7-9 hours after egg laying).1 Publication

Structurei

3D structure databases

ProteinModelPortaliP39205.
SMRiP39205. Positions 7-156, 198-592.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni3 – 153151MPT adenylyltransferaseAdd
BLAST
Regioni184 – 596413MPT Mo-transferaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the MoaB/Mog family.Curated
In the C-terminal section; belongs to the MoeA family.Curated

Phylogenomic databases

eggNOGiCOG0303.
GeneTreeiENSGT00390000016577.
HOGENOMiHOG000218563.
InParanoidiP39205.
KOiK15376.
OMAiGGIWDTN.
OrthoDBiEOG70087N.
PhylomeDBiP39205.

Family and domain databases

Gene3Di2.40.340.10. 1 hit.
3.40.980.10. 2 hits.
InterProiIPR020817. Mo_cofactor_synthesis.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_linker/N.
IPR001453. Mopterin-bd_dom.
[Graphical view]
PfamiPF00994. MoCF_biosynth. 2 hits.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view]
SMARTiSM00852. MoCF_biosynth. 2 hits.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 2 hits.
SSF63867. SSF63867. 1 hit.
SSF63882. SSF63882. 1 hit.
TIGRFAMsiTIGR00177. molyb_syn. 2 hits.
PROSITEiPS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39205-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESITFGVLT ISDTCWQEPE KDTSGPILRQ LIGETFANTQ VIGNIVPDEK
60 70 80 90 100
DIIQQELRKW IDREELRVIL TTGGTGFAPR DVTPEATRQL LEKECPQLSM
110 120 130 140 150
YITLESIKQT QYAALSRGLC GIAGNTLILN LPGSEKAVKE CFQTISALLP
160 170 180 190 200
HAVHLIGDDV SLVRKTHAEV QGSAQKSHIC PHKTGTGTDS DRNSPYPMLP
210 220 230 240 250
VQEVLSIIFN TVQKTANLNK ILLEMNAPVN IPPFRASIKD GYAMKSTGFS
260 270 280 290 300
GTKRVLGCIA AGDSPNSLPL AEDECYKINT GAPLPLEADC VVQVEDTKLL
310 320 330 340 350
QLDKNGQESL VDILVEPQAG LDVRPVGYDL STNDRIFPAL DPSPVVVKSL
360 370 380 390 400
LASVGNRLIL SKPKVAIVST GSELCSPRNQ LTPGKIFDSN TTMLTELLVY
410 420 430 440 450
FGFNCMHTCV LSDSFQRTKE SLLELFEVVD FVICSGGVSM GDKDFVKSVL
460 470 480 490 500
EDLQFRIHCG RVNIKPGKPM TFASRKDKYF FGLPGNPVSA FVTFHLFALP
510 520 530 540 550
AIRFAAGWDR CKCSLSVLNV KLLNDFSLDS RPEFVRASVI SKSGELYASV
560 570 580 590 600
NGNQISSRLQ SIVGADVLIN LPARTSDRPL AKAGEIFPAS VLRFDFISKY

E
Length:601
Mass (Da):65,733
Last modified:January 23, 2007 - v3
Checksum:iDFA6926E955BF287
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti414 – 4141S → T in AAA65877 (PubMed:8088525).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19876 mRNA. Translation: AAA65877.1.
AE014298 Genomic DNA. Translation: AAN09010.1.
AL050231 Genomic DNA. Translation: CAB65851.1. Sequence problems.
AL050231 Genomic DNA. Translation: CAB65852.1.
AY069078 mRNA. Translation: AAL39223.1.
PIRiS47896.
RefSeqiNP_477030.1. NM_057682.4.
UniGeneiDm.2294.

Genome annotation databases

EnsemblMetazoaiFBtr0070064; FBpp0070063; FBgn0000316.
FBtr0070065; FBpp0070064; FBgn0000316.
GeneIDi30973.
KEGGidme:Dmel_CG2945.
UCSCiCG2945-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19876 mRNA. Translation: AAA65877.1.
AE014298 Genomic DNA. Translation: AAN09010.1.
AL050231 Genomic DNA. Translation: CAB65851.1. Sequence problems.
AL050231 Genomic DNA. Translation: CAB65852.1.
AY069078 mRNA. Translation: AAL39223.1.
PIRiS47896.
RefSeqiNP_477030.1. NM_057682.4.
UniGeneiDm.2294.

3D structure databases

ProteinModelPortaliP39205.
SMRiP39205. Positions 7-156, 198-592.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiP39205.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070064; FBpp0070063; FBgn0000316.
FBtr0070065; FBpp0070064; FBgn0000316.
GeneIDi30973.
KEGGidme:Dmel_CG2945.
UCSCiCG2945-RA. d. melanogaster.

Organism-specific databases

CTDi30973.
FlyBaseiFBgn0000316. cin.

Phylogenomic databases

eggNOGiCOG0303.
GeneTreeiENSGT00390000016577.
HOGENOMiHOG000218563.
InParanoidiP39205.
KOiK15376.
OMAiGGIWDTN.
OrthoDBiEOG70087N.
PhylomeDBiP39205.

Enzyme and pathway databases

UniPathwayiUPA00344.
ReactomeiREACT_180227. Molybdenum cofactor biosynthesis.

Miscellaneous databases

GenomeRNAii30973.
NextBioi771251.
PROiP39205.

Family and domain databases

Gene3Di2.40.340.10. 1 hit.
3.40.980.10. 2 hits.
InterProiIPR020817. Mo_cofactor_synthesis.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_linker/N.
IPR001453. Mopterin-bd_dom.
[Graphical view]
PfamiPF00994. MoCF_biosynth. 2 hits.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view]
SMARTiSM00852. MoCF_biosynth. 2 hits.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 2 hits.
SSF63867. SSF63867. 1 hit.
SSF63882. SSF63882. 1 hit.
TIGRFAMsiTIGR00177. molyb_syn. 2 hits.
PROSITEiPS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila molybdenum cofactor gene cinnamon is homologous to three Escherichia coli cofactor proteins and to the rat protein gephyrin."
    Kamdar K.P., Shelton M.E., Finnerty V.
    Genetics 137:791-801(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. "The Drosophila cinnamon gene is functionally homologous to Arabidopsis cnx1 and has a similar expression pattern to the mammalian gephyrin gene."
    Wittle A.E., Kamdar K.P., Finnerty V.
    Mol. Gen. Genet. 261:672-680(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
    Strain: Canton-S.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Oregon-R.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  7. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCIN_DROME
AccessioniPrimary (citable) accession number: P39205
Secondary accession number(s): Q0KHX9, Q9U1M0, Q9V3E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.