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Protein

Methylthioribose-1-phosphate isomerase

Gene

Mri1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).UniRule annotation

Catalytic activityi

S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate.UniRule annotation

Pathwayi: L-methionine biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate.UniRule annotation
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Methylthioribose-1-phosphate isomerase (Mri1)
  2. Methylthioribulose-1-phosphate dehydratase (Apip)
  3. Enolase-phosphatase E1 (Enoph1)
  4. Enolase-phosphatase E1 (Enoph1)
  5. 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (Adi1), 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (Adi1)
  6. no protein annotated in this organism
This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate, the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei168 – 1681Transition state stabilizerUniRule annotation
Active sitei248 – 2481Proton donorUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Enzyme and pathway databases

ReactomeiR-MMU-1237112. Methionine salvage pathway.
UniPathwayiUPA00904; UER00874.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylthioribose-1-phosphate isomeraseUniRule annotation (EC:5.3.1.23UniRule annotation)
Short name:
M1PiUniRule annotation
Short name:
MTR-1-P isomeraseUniRule annotation
Alternative name(s):
S-methyl-5-thioribose-1-phosphate isomeraseUniRule annotation
Translation initiation factor eIF-2B subunit alpha/beta/delta-like proteinUniRule annotation
Gene namesi
Name:Mri1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1915123. Mri1.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 369369Methylthioribose-1-phosphate isomerasePRO_0000317326Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei366 – 3661PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CQT1.
MaxQBiQ9CQT1.
PaxDbiQ9CQT1.
PRIDEiQ9CQT1.

PTM databases

iPTMnetiQ9CQT1.
PhosphoSiteiQ9CQT1.

Expressioni

Gene expression databases

BgeeiQ9CQT1.
CleanExiMM_2410018C20RIK.
ExpressionAtlasiQ9CQT1. baseline and differential.
GenevisibleiQ9CQT1. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9CQT1. 2 interactions.
MINTiMINT-4124975.
STRINGi10090.ENSMUSP00000122623.

Structurei

3D structure databases

ProteinModelPortaliQ9CQT1.
SMRiQ9CQT1. Positions 2-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eIF-2B alpha/beta/delta subunits family. MtnA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG1468. Eukaryota.
COG0182. LUCA.
GeneTreeiENSGT00390000013732.
InParanoidiQ9CQT1.
KOiK08963.
OMAiAIPGGDH.
OrthoDBiEOG7SBNP2.
PhylomeDBiQ9CQT1.
TreeFamiTF300852.

Family and domain databases

Gene3Di1.20.120.420. 1 hit.
HAMAPiMF_01678. Salvage_MtnA.
InterProiIPR000649. IF-2B-related.
IPR005251. IF-M1Pi.
IPR011559. Initiation_fac_2B_a/b/d.
IPR027363. M1Pi_N.
[Graphical view]
PfamiPF01008. IF-2B. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00524. eIF-2B_rel. 1 hit.
TIGR00512. salvage_mtnA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9CQT1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLEAIRYSP GSLQILDQLQ LPEHCHYEAL SSVQQASEAI RAMKVRGAPA
60 70 80 90 100
IALVGCLSLA VELRAGAGGP GLAALVAFVR DQLRLLVAAR PTAVNMARAA
110 120 130 140 150
RDLGQVAAQE AEREGATEET VRERVIRFAE DMLEKDLKDN RSIGDLGARH
160 170 180 190 200
LLEQTNPRGG KVTVLTHCNT GALATAGYGT ALGVIRSLHE MGRLEHTFCT
210 220 230 240 250
ETRPYNQGAR LTAFELVYEQ IPATLITDSM AAAAMAHRGV SAVVVGADRV
260 270 280 290 300
VANGDTANKI GTYQLAIVAK HHGVPFYVAA PSSSCDLHLE TGKEIVIEER
310 320 330 340 350
PSQELTDLNG VRIAAQGIRV WNPAFDVTPH ELITGGIITE LGVFAPEELR
360
GALSASVFSE GQTLDSPWV
Length:369
Mass (Da):39,411
Last modified:June 1, 2001 - v1
Checksum:i5DEA57F8E4AE99E0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti168 – 1681C → L in BAC33016 (PubMed:16141072).Curated
Sequence conflicti190 – 1901E → D in BAC33016 (PubMed:16141072).Curated
Sequence conflicti238 – 2381R → Q in BAC33016 (PubMed:16141072).Curated
Sequence conflicti291 – 2911T → S in BAC33016 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010538 mRNA. Translation: BAB27014.1.
AK013882 mRNA. Translation: BAB29034.1.
AK164894 mRNA. Translation: BAE37957.1.
AK047287 mRNA. Translation: BAC33016.1.
BC025049 mRNA. Translation: AAH25049.1.
CCDSiCCDS22473.1.
RefSeqiNP_080699.3. NM_026423.4.
UniGeneiMm.278085.

Genome annotation databases

EnsembliENSMUST00000126435; ENSMUSP00000122623; ENSMUSG00000004996.
GeneIDi67873.
KEGGimmu:67873.
UCSCiuc009mmi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010538 mRNA. Translation: BAB27014.1.
AK013882 mRNA. Translation: BAB29034.1.
AK164894 mRNA. Translation: BAE37957.1.
AK047287 mRNA. Translation: BAC33016.1.
BC025049 mRNA. Translation: AAH25049.1.
CCDSiCCDS22473.1.
RefSeqiNP_080699.3. NM_026423.4.
UniGeneiMm.278085.

3D structure databases

ProteinModelPortaliQ9CQT1.
SMRiQ9CQT1. Positions 2-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CQT1. 2 interactions.
MINTiMINT-4124975.
STRINGi10090.ENSMUSP00000122623.

PTM databases

iPTMnetiQ9CQT1.
PhosphoSiteiQ9CQT1.

Proteomic databases

EPDiQ9CQT1.
MaxQBiQ9CQT1.
PaxDbiQ9CQT1.
PRIDEiQ9CQT1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000126435; ENSMUSP00000122623; ENSMUSG00000004996.
GeneIDi67873.
KEGGimmu:67873.
UCSCiuc009mmi.2. mouse.

Organism-specific databases

CTDi84245.
MGIiMGI:1915123. Mri1.

Phylogenomic databases

eggNOGiKOG1468. Eukaryota.
COG0182. LUCA.
GeneTreeiENSGT00390000013732.
InParanoidiQ9CQT1.
KOiK08963.
OMAiAIPGGDH.
OrthoDBiEOG7SBNP2.
PhylomeDBiQ9CQT1.
TreeFamiTF300852.

Enzyme and pathway databases

UniPathwayiUPA00904; UER00874.
ReactomeiR-MMU-1237112. Methionine salvage pathway.

Miscellaneous databases

NextBioi325797.
PROiQ9CQT1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQT1.
CleanExiMM_2410018C20RIK.
ExpressionAtlasiQ9CQT1. baseline and differential.
GenevisibleiQ9CQT1. MM.

Family and domain databases

Gene3Di1.20.120.420. 1 hit.
HAMAPiMF_01678. Salvage_MtnA.
InterProiIPR000649. IF-2B-related.
IPR005251. IF-M1Pi.
IPR011559. Initiation_fac_2B_a/b/d.
IPR027363. M1Pi_N.
[Graphical view]
PfamiPF01008. IF-2B. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00524. eIF-2B_rel. 1 hit.
TIGR00512. salvage_mtnA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Head and Lung.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiMTNA_MOUSE
AccessioniPrimary (citable) accession number: Q9CQT1
Secondary accession number(s): Q8BXF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 117 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.