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P22033 (MUTA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylmalonyl-CoA mutase, mitochondrial
Short name=MCM
EC=5.4.99.2
Alternative name(s):
Methylmalonyl-CoA isomerase
Gene names
Name:MUT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length750 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the degradation of several amino acids, odd-chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species.

Catalytic activity

(R)-methylmalonyl-CoA = succinyl-CoA.

Cofactor

Adenosylcobalamin.

Subunit structure

Homodimer.

Subcellular location

Mitochondrion matrix.

Involvement in disease

Methylmalonic aciduria type mut (MMAM) [MIM:251000]: An often fatal disorder of organic acid metabolism. Common clinical features include lethargy, vomiting, failure to thrive, hypotonia, neurological deficit and early death. Two forms of the disease are distinguished by the presence (mut-) or absence (mut0) of residual enzyme activity. Mut0 patients have more severe neurological manifestations of the disease than do MUT- patients. MMAM is unresponsive to vitamin B12 therapy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21

Sequence similarities

Belongs to the methylmalonyl-CoA mutase family.

Contains 1 B12-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Mitochondrion
Chain33 – 750718Methylmalonyl-CoA mutase, mitochondrial
PRO_0000019293

Regions

Domain614 – 746133B12-binding

Sites

Metal binding6271Cobalt (cobalamin axial ligand) By similarity

Natural variations

Natural variant691I → V. Ref.20 Ref.21
VAR_023472
Natural variant861P → L in MMAM; mut0. Ref.21
VAR_026592
Natural variant871G → E in MMAM; mut0. Ref.21
VAR_026593
Natural variant931R → H in MMAM; mut0. Ref.8 Ref.21
VAR_004409
Natural variant941G → R in MMAM; mut0. Ref.21
VAR_026594
Natural variant941G → V in MMAM; mut- and mut0. Ref.13 Ref.21
VAR_022393
Natural variant951P → R in MMAM; mut0. Ref.21
VAR_026595
Natural variant1051W → R in MMAM; mut0. Ref.7 Ref.21
VAR_004410
Natural variant1081R → C in MMAM; mut0. Ref.21
VAR_026596
Natural variant1081R → G in MMAM; mut-. Ref.21
VAR_026597
Natural variant1081R → H in MMAM; mut0. Ref.19 Ref.21
VAR_022394
Natural variant1091Q → R in MMAM; mut0. Ref.20
VAR_023473
Natural variant1371A → V in MMAM; mut0. Ref.17
VAR_022395
Natural variant1451G → S in MMAM; mut0. Ref.21
VAR_026598
Natural variant1481S → L in MMAM. Ref.19
VAR_022396
Natural variant1561D → N in MMAM; mut-. Ref.19
VAR_022397
Natural variant1581G → V in MMAM; mut0. Ref.19
VAR_022398
Natural variant1741F → S in MMAM; mut0. Ref.17 Ref.21
VAR_022399
Natural variant1861M → V in MMAM; mut-. Ref.21
VAR_026599
Natural variant1891N → K in MMAM; mut-. Ref.21
VAR_026600
Natural variant1911A → E in MMAM; mut- and mut0. Ref.16 Ref.19 Ref.20 Ref.21
VAR_004411
Natural variant1971A → E in MMAM; mut0. Ref.21
VAR_026601
Natural variant2031G → R in MMAM; mut0. Ref.17 Ref.19 Ref.21
VAR_022400
Natural variant2151G → C in MMAM; mut- and mut0. Ref.21
VAR_026602
Natural variant2151G → S in MMAM; mut0. Ref.19 Ref.21
VAR_022401
Natural variant2181Q → H in MMAM; mut0. Ref.17 Ref.21
VAR_022402
Natural variant2191N → Y in MMAM; mut0. Ref.18 Ref.19 Ref.20 Ref.21
VAR_022403
Natural variant2281R → Q in MMAM; mut0. Ref.16 Ref.21
VAR_004412
Natural variant2301T → I in MMAM; mut-. Ref.21
VAR_026603
Natural variant2311Y → N in MMAM; mut-. Ref.13 Ref.21
VAR_004413
Natural variant2621S → N in MMAM; mut0. Ref.19 Ref.21
VAR_022404
Natural variant2651H → Y in MMAM; mut-. Ref.21
VAR_026604
Natural variant2811L → S in MMAM; mut0. Ref.21
VAR_026605
Natural variant2911G → E in MMAM; mut0. Ref.21
VAR_026606
Natural variant2931Q → P in MMAM; mut0. Ref.19
VAR_022405
Natural variant3051L → S in MMAM; mut0. Ref.21
VAR_026607
Natural variant3061S → F in MMAM; mut0. Ref.21
VAR_026608
Natural variant3121G → V in MMAM; mut0. Ref.16 Ref.21
VAR_004414
Natural variant3161Y → C in MMAM; mut-. Ref.21
VAR_026609
Natural variant3241A → T in MMAM; mut-. Ref.20 Ref.21
VAR_023474
Natural variant3281L → F in MMAM; mut0. Ref.19
VAR_022406
Natural variant3281L → P in MMAM; mut0. Ref.20
VAR_023475
Natural variant3461Missing in MMAM; mut0. Ref.16 Ref.21
VAR_004415
Natural variant3471L → R in MMAM; mut0. Ref.21
VAR_026610
Natural variant3501H → Y in MMAM; mut0. Ref.21
VAR_026611
Natural variant3681V → D in MMAM.
VAR_004416
Natural variant3691R → C in MMAM; mut0. Ref.21
VAR_026612
Natural variant3691R → H in MMAM; mut- and mut0. Ref.13 Ref.21
VAR_004417
Natural variant3701T → P in MMAM; mut0. Ref.21
VAR_026613
Natural variant3771A → E in MMAM; mut0. Ref.7 Ref.21
VAR_004418
Natural variant3831Q → H in MMAM; mut0. Ref.21
VAR_026614
Natural variant3831Q → P in MMAM; mut0. Ref.21
VAR_026615
Natural variant3861H → N in MMAM; mut0. Ref.21
VAR_026616
Natural variant3881N → H in MMAM; mut0. Ref.21
VAR_026617
Natural variant3891Missing in MMAM; mut0. Ref.21
VAR_026618
Natural variant4121Missing in MMAM; mut0. Ref.21
VAR_026619
Natural variant4261G → R in MMAM; mut-. Ref.21
VAR_026620
Natural variant4271G → D in MMAM; mut0. Ref.21
VAR_026621
Natural variant4991A → T. Ref.4 Ref.6 Ref.18 Ref.21
Corresponds to variant rs2229385 [ dbSNP | Ensembl ].
VAR_022407
Natural variant5181L → P in MMAM; mut0. Ref.21
VAR_026622
Natural variant5321R → H. Ref.1 Ref.2 Ref.11 Ref.21
Corresponds to variant rs1141321 [ dbSNP | Ensembl ].
VAR_004419
Natural variant5351A → P in MMAM; mut0. Ref.17
VAR_022408
Natural variant5601C → Y in MMAM; mut0. Ref.21
VAR_026623
Natural variant5661T → R in MMAM; mut0. Ref.21
VAR_026624
Natural variant5731F → S in MMAM; mut-. Ref.21
VAR_026625
Natural variant5871Y → C in MMAM; mut-. Ref.19
VAR_022409
Natural variant5981T → A.
Corresponds to variant rs9473556 [ dbSNP | Ensembl ].
VAR_030495
Natural variant6151P → R in MMAM; mut0. Ref.21
VAR_026626
Natural variant6151P → T in MMAM; mut0. Ref.19
VAR_022410
Natural variant6161R → C in MMAM; mut0. Ref.20 Ref.21
VAR_023476
Natural variant6171L → R in MMAM. Ref.20
VAR_023477
Natural variant6211K → N in MMAM; mut0. Ref.19
VAR_022411
Natural variant6231G → R in MMAM; mut0. Ref.12 Ref.13 Ref.19 Ref.21
VAR_004420
Natural variant6241Q → R in MMAM. Ref.19
VAR_022412
Natural variant6261G → C in MMAM; mut-. Ref.11
VAR_004421
Natural variant6271H → R in MMAM; mut0. Ref.17 Ref.19
VAR_022413
Natural variant6301G → E in MMAM; mut0. Ref.11 Ref.21
VAR_004422
Natural variant6331V → G in MMAM; mut-. Ref.16 Ref.21
VAR_004423
Natural variant6371G → E in MMAM; mut-. Ref.19
VAR_022414
Natural variant6371G → R in MMAM; mut0. Ref.21
VAR_026627
Natural variant6381F → I in MMAM; mut0. Ref.19
VAR_022415
Natural variant6401D → Y in MMAM; mut0. Ref.19
VAR_022416
Natural variant6421G → R in MMAM; mut-. Ref.19 Ref.21
VAR_022417
Natural variant6481G → D in MMAM; mut-. Ref.11
VAR_004424
Natural variant6691V → E in MMAM; mut0.
VAR_004425
Natural variant6711I → V. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.9 Ref.10 Ref.15 Ref.18 Ref.21 Ref.22
Corresponds to variant rs8589 [ dbSNP | Ensembl ].
VAR_004426
Natural variant6781H → R in MMAM; mut-. Ref.13 Ref.21
VAR_004427
Natural variant6841E → EL in MMAM; mut-. Ref.16
VAR_004428
Natural variant6851L → R in MMAM; mut-. Ref.16 Ref.21
VAR_004429
Natural variant6941R → W in MMAM; mut- and mut0. Ref.11 Ref.13 Ref.19 Ref.21
VAR_004430
Natural variant7001M → K in MMAM; mut-. Ref.19 Ref.21
VAR_022418
Natural variant7031G → R in MMAM; mut0. Ref.12 Ref.21
VAR_004431
Natural variant7171G → V in MMAM; mut-; interfers with the binding of the cofactor to the apoenzyme. Ref.9 Ref.10 Ref.13 Ref.15 Ref.21
VAR_004432

Experimental info

Sequence conflict1531V → L in AAA99226. Ref.2
Sequence conflict2361E → D in AAA99226. Ref.2
Sequence conflict274 – 2774ILEL → FWSW in AAA99226. Ref.2
Sequence conflict3161Y → H in AAA99226. Ref.2
Sequence conflict5051I → T in AAA99226. Ref.2
Sequence conflict5161E → G in AAA99226. Ref.2
Sequence conflict5911F → Y in AAA99226. Ref.2

Secondary structure

1 ..................................................................................................................... 750
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22033 [UniParc].

Last modified January 11, 2011. Version 4.
Checksum: B5909729C08B562F

FASTA75083,134
        10         20         30         40         50         60 
MLRAKNQLFL LSPHYLRQVK ESSGSRLIQQ RLLHQQQPLH PEWAALAKKQ LKGKNPEDLI 

        70         80         90        100        110        120 
WHTPEGISIK PLYSKRDTMD LPEELPGVKP FTRGPYPTMY TFRPWTIRQY AGFSTVEESN 

       130        140        150        160        170        180 
KFYKDNIKAG QQGLSVAFDL ATHRGYDSDN PRVRGDVGMA GVAIDTVEDT KILFDGIPLE 

       190        200        210        220        230        240 
KMSVSMTMNG AVIPVLANFI VTGEEQGVPK EKLTGTIQND ILKEFMVRNT YIFPPEPSMK 

       250        260        270        280        290        300 
IIADIFEYTA KHMPKFNSIS ISGYHMQEAG ADAILELAYT LADGLEYSRT GLQAGLTIDE 

       310        320        330        340        350        360 
FAPRLSFFWG IGMNFYMEIA KMRAGRRLWA HLIEKMFQPK NSKSLLLRAH CQTSGWSLTE 

       370        380        390        400        410        420 
QDPYNNIVRT AIEAMAAVFG GTQSLHTNSF DEALGLPTVK SARIARNTQI IIQEESGIPK 

       430        440        450        460        470        480 
VADPWGGSYM MECLTNDVYD AALKLINEIE EMGGMAKAVA EGIPKLRIEE CAARRQARID 

       490        500        510        520        530        540 
SGSEVIVGVN KYQLEKEDAV EVLAIDNTSV RNRQIEKLKK IKSSRDQALA ERCLAALTEC 

       550        560        570        580        590        600 
AASGDGNILA LAVDASRARC TVGEITDALK KVFGEHKAND RMVSGAYRQE FGESKEITSA 

       610        620        630        640        650        660 
IKRVHKFMER EGRRPRLLVA KMGQDGHDRG AKVIATGFAD LGFDVDIGPL FQTPREVAQQ 

       670        680        690        700        710        720 
AVDADVHAVG ISTLAAGHKT LVPELIKELN SLGRPDILVM CGGVIPPQDY EFLFEVGVSN 

       730        740        750 
VFGPGTRIPK AAVQVLDDIE KCLEKKQQSV

« Hide

References

« Hide 'large scale' references
[1]"Cloning of full-length methylmalonyl-CoA mutase from a cDNA library using the polymerase chain reaction."
Jansen R., Kalousek F., Fenton W.A., Rosenberg L.E., Ledley F.D.
Genomics 4:198-205(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANTS HIS-532 AND VAL-671.
Tissue: Liver.
[2]"Structure of the human methylmalonyl-CoA mutase (MUT) locus."
Nham S.U., Wilkemeyer M.F., Ledley F.D.
Genomics 8:710-716(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-532 AND VAL-671.
[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. expand/collapse author list , 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], VARIANT VAL-671.
Tissue: Testis.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS THR-499 AND VAL-671.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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], VARIANTS THR-499 AND VAL-671.
Tissue: Uterus.
[7]"Heterozygous mutations at the mut locus in fibroblasts with mut0 methylmalonic acidemia identified by polymerase-chain-reaction cDNA cloning."
Jansen R., Ledley F.D.
Am. J. Hum. Genet. 47:808-814(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MMAM ARG-105 AND GLU-377.
[8]"Genetic characterization of a MUT locus mutation discriminating heterogeneity in mut0 and mut- methylmalonic aciduria by interallelic complementation."
Raff M.L., Crane A.M., Jansen R., Ledley F.D., Rosenblatt D.S.
J. Clin. Invest. 87:203-207(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MMAM HIS-93.
[9]"Phenotype of disease in three patients with identical mutations in methylmalonyl CoA mutase."
Crane A.M., Martin L.S., Valle D., Ledley F.D.
Hum. Genet. 89:259-264(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MMAM VAL-717, VARIANT VAL-671.
[10]"Cloning and expression of a mutant methylmalonyl coenzyme A mutase with altered cobalamin affinity that causes mut- methylmalonic aciduria."
Crane A.M., Jansen R., Andrews E.R., Ledley F.D.
J. Clin. Invest. 89:385-391(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MMAM VAL-717, VARIANT VAL-671.
[11]"Clustering of mutations in methylmalonyl CoA mutase associated with mut-methylmalonic acidemia."
Crane A.M., Ledley F.D.
Am. J. Hum. Genet. 55:42-50(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MMAM CYS-626; GLU-630; ASP-648 AND TRP-694, VARIANT HIS-532.
[12]"Cloning and expression of mutations demonstrating intragenic complementation in mut0 methylmalonic aciduria."
Qureshi A.A., Crane A.M., Matiaszuk N.V., Resvani I., Ledley F.D., Rosenblatt D.S.
J. Clin. Invest. 93:1812-1819(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MMAM ARG-623 AND ARG-703.
[13]"Expression and kinetic characterization of methylmalonyl-CoA mutase from patients with the mut- phenotype: evidence for naturally occurring interallelic complementation."
Janata J., Kogekar N., Fenton W.A.
Hum. Mol. Genet. 6:1457-1464(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MMAM VAL-94; ASN-231; HIS-369; ARG-623; ARG-678; TRP-694 AND VAL-717.
[14]"Mutations in mut methylmalonic acidemia: clinical and enzymatic correlations."
Ledley F.D., Rosenblatt D.S.
Hum. Mutat. 9:1-6(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[15]"A common mutation among blacks with mut- methylmalonic aciduria."
Adjalla C.E., Hosack A.R., Matiaszuk N.V., Rosenblatt D.S.
Hum. Mutat. Suppl. 1:S248-S250(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MMAM VAL-717, VARIANT VAL-671.
[16]"Seven novel mutations in mut methylmalonic aciduria."
Adjalla C.E., Hosack A.R., Gilfix B.M., Lamothe E., Sun S., Chan A., Evans S., Matiaszuk N.V., Rosenblatt D.S.
Hum. Mutat. 11:270-274(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MMAM GLU-191; GLN-228; VAL-312; LEU-346 DEL; GLY-633; LEU-684 INS AND ARG-685.
[17]"mut0 methylmalonic acidemia: eleven novel mutations of the methylmalonyl CoA mutase including a deletion-insertion mutation."
Fuchshuber A., Mucha B., Baumgartner E.R., Vollmer M., Hildebrandt F.
Hum. Mutat. 16:179-179(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MMAM VAL-137; SER-174; ARG-203; HIS-218; PRO-535 AND ARG-627.
[18]"Mutation analysis of the MCM gene in Israeli patients with mut(0) disease."
Berger I., Shaag A., Anikster Y., Baumgartner E.R., Bar-Meir M., Joseph A., Elpeleg O.N.
Mol. Genet. Metab. 73:107-110(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MMAM TYR-219, VARIANTS THR-499 AND VAL-671.
[19]"Molecular basis of methylmalonyl-CoA mutase apoenzyme defect in 40 European patients affected by mut(o) and mut- forms of methylmalonic acidemia: identification of 29 novel mutations in the MUT gene."
Acquaviva C., Benoist J.-F., Pereira S., Callebaut I., Koskas T., Porquet D., Elion J.
Hum. Mutat. 25:167-176(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MMAM HIS-108; LEU-148; ASN-156; VAL-158; GLU-191; ARG-203; SER-215; TYR-219; ASN-262; PRO-293; PHE-328; CYS-587; THR-615; ASN-621; ARG-623; ARG-624; ARG-627; GLU-637; ILE-638; TYR-640; ARG-642; TRP-694 AND LYS-700.
[20]"Genetic analysis of three genes causing isolated methylmalonic acidemia: identification of 21 novel allelic variants."
Martinez M.A., Rincon A., Desviat L.R., Merinero B., Ugarte M., Perez B.
Mol. Genet. Metab. 84:317-325(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MMAM ARG-109; GLU-191; TYR-219; THR-324; PRO-328; CYS-616 AND ARG-617, VARIANT VAL-69.
[21]"Spectrum of mutations in mut methylmalonic acidemia and identification of a common Hispanic mutation and haplotype."
Worgan L.C., Niles K., Tirone J.C., Hofmann A., Verner A., Sammak A., Kucic T., Lepage P., Rosenblatt D.S.
Hum. Mutat. 27:31-43(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MMAM LEU-86; GLU-87; HIS-93; ARG-94; VAL-94; ARG-95; ARG-105; CYS-108; GLY-108; HIS-108; SER-145; SER-174; VAL-186; LYS-189; GLU-191; GLU-197; ARG-203; CYS-215; SER-215; HIS-218; TYR-219; GLN-228; ILE-230; ASN-231; ASN-262; TYR-265; SER-281; GLU-291; SER-305; PHE-306; VAL-312; CYS-316; THR-324; LEU-346 DEL; ARG-347; TYR-350; CYS-369; HIS-369; PRO-370; GLU-377; HIS-383; PRO-383; ASN-386; HIS-388; SER-389 DEL; ILE-412 DEL; ARG-426; ASP-427; PRO-518; TYR-560; ARG-566; SER-573; ARG-615; CYS-616; ARG-623; GLU-630; GLY-633; ARG-637; ARG-642; ARG-678; ARG-685; TRP-694; LYS-700; ARG-703 AND VAL-717, VARIANTS VAL-69; THR-499; HIS-532 AND VAL-671.
[22]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-671, MASS SPECTROMETRY.
+Additional computationally mapped references.

Web resources

GeneReviews
Wikipedia

Methylmalonyl coenzyme A mutase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M65131 mRNA. Translation: AAA59569.1.
M37510 expand/collapse EMBL AC list , M37499, M37500, M37501, M37503, M37504, M37505, M37506, M37507, M37508, M37509 Genomic DNA. Translation: AAA99226.1.
AK292568 mRNA. Translation: BAF85257.1.
BT007434 mRNA. Translation: AAP36102.1.
AL590668 Genomic DNA. Translation: CAI14311.1.
BC016282 mRNA. Translation: AAH16282.1.
IPIIPI00024934.
PIRA59145.
RefSeqNP_000246.2. NM_000255.3.
UniGeneHs.485527.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XIJX-ray1.95A12-750[»]
2XIQX-ray1.95A/B12-750[»]
3BICX-ray2.60A/B12-750[»]
ProteinModelPortalP22033.
SMRP22033. Positions 36-749.
ModBaseSearch...

Protein-protein interaction databases

IntActP22033. 1 interaction.
STRING9606.ENSP00000274813.

PTM databases

PhosphoSiteP22033.

Polymorphism databases

DMDM67469281.

Proteomic databases

PaxDbP22033.
PRIDEP22033.

Protocols and materials databases

DNASU4594.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000274813; ENSP00000274813; ENSG00000146085.
GeneID4594.
KEGGhsa:4594.
UCSCuc003ozg.4. human.

Organism-specific databases

CTD4594.
GeneCardsGC06M049445.
H-InvDBHIX0005945.
HGNCHGNC:7526. MUT.
HPAHPA035971.
MIM251000. phenotype.
609058. gene.
neXtProtNX_P22033.
Orphanet289916. Complete deficiency of methylmalonyl-CoA mutase.
79312. Partial deficiency of methylmalonyl-CoA mutase.
PharmGKBPA31327.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2185.
HOGENOMHOG000003917.
HOVERGENHBG006423.
InParanoidP22033.
KOK01847.
OMANDVHILG.
OrthoDBEOG45X7VJ.
PhylomeDBP22033.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP22033.

Gene expression databases

BgeeP22033.
CleanExHS_MUT.
GenevestigatorP22033.
GermOnlineENSG00000146085. Homo sapiens.

Family and domain databases

Gene3D3.20.20.240. 1 hit.
3.40.50.280. 1 hit.
InterProIPR006159. Acid_CoA_mut_C.
IPR016176. Cbl-dep_enz_cat.
IPR014348. Cbl-dep_enz_cat-sub.
IPR006158. Cobalamin-bd.
IPR006099. MeMalonylCoA_mutase_a/b_cat.
IPR006098. MMCoA_mutase_a_cat.
[Graphical view]
PfamPF02310. B12-binding. 1 hit.
PF01642. MM_CoA_mutase. 1 hit.
[Graphical view]
SUPFAMSSF52242. Cbl-bd. 1 hit.
SSF51703. Cbl-dep_enz_cat. 1 hit.
TIGRFAMsTIGR00640. acid_CoA_mut_C. 1 hit.
TIGR00641. acid_CoA_mut_N. 1 hit.
PROSITEPS51332. B12_BINDING. 1 hit.
PS00544. METMALONYL_COA_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.
EvolutionaryTraceP22033.
GenomeRNAi4594.
NextBio17660.
SOURCESearch...

Entry information

Entry nameMUTA_HUMAN
AccessionPrimary (citable) accession number: P22033
Secondary accession number(s): A8K953 expand/collapse secondary AC list , Q5SYZ3, Q96B11, Q9UD64
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 11, 2011
Last modified: May 1, 2013
This is version 146 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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