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Protein

Methylmalonyl-CoA mutase, mitochondrial

Gene

MUT

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

Functioni

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 activityi

(R)-methylmalonyl-CoA = succinyl-CoA.1 Publication

Cofactori

Kineticsi

  1. KM=4.7 nM for adenosylcob(III)alamin1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi627 – 6271Cobalt (cobalamin axial ligand)By similarity

    GO - Molecular functioni

    • cobalamin binding Source: UniProtKB-KW
    • metal ion binding Source: UniProtKB-KW
    • methylmalonyl-CoA mutase activity Source: ProtInc
    • modified amino acid binding Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Cobalamin, Cobalt, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07322-MONOMER.
    BRENDAi5.4.99.2. 2681.
    ReactomeiR-HSA-196741. Cobalamin (Cbl, vitamin B12) transport and metabolism.
    R-HSA-3359475. Defective MMAA causes methylmalonic aciduria type cblA.
    R-HSA-3359478. Defective MUT causes methylmalonic aciduria mut type.
    R-HSA-71032. Propionyl-CoA catabolism.
    SABIO-RKP22033.

    Chemistry

    SwissLipidsiSLP:000001254.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methylmalonyl-CoA mutase, mitochondrial (EC:5.4.99.21 Publication)
    Short name:
    MCM
    Alternative name(s):
    Methylmalonyl-CoA isomerase
    Gene namesi
    Name:MUT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:7526. MUT.

    Subcellular locationi

    GO - Cellular componenti

    • mitochondrial matrix Source: Reactome
    • mitochondrion Source: ProtInc
    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Methylmalonic aciduria type mut (MMAM)17 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn 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.
    See also OMIM:251000
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti86 – 861P → L in MMAM; mut0 and mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 2 Publications
    VAR_026592
    Natural varianti87 – 871G → E in MMAM; mut0. 1 Publication
    VAR_026593
    Natural varianti93 – 931R → H in MMAM; mut0. 3 Publications
    Corresponds to variant rs121918251 [ dbSNP | Ensembl ].
    VAR_004409
    Natural varianti94 – 941G → R in MMAM; mut0. 1 Publication
    VAR_026594
    Natural varianti94 – 941G → V in MMAM; mut- and mut0. 2 Publications
    VAR_022393
    Natural varianti95 – 951P → R in MMAM; mut0. 1 Publication
    VAR_026595
    Natural varianti100 – 1001Y → C in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 2 Publications
    VAR_075379
    Natural varianti105 – 1051W → R in MMAM; mut0. 2 Publications
    VAR_004410
    Natural varianti108 – 1081R → C in MMAM; mut0. 2 Publications
    Corresponds to variant rs121918257 [ dbSNP | Ensembl ].
    VAR_026596
    Natural varianti108 – 1081R → G in MMAM; mut-. 1 Publication
    VAR_026597
    Natural varianti108 – 1081R → H in MMAM; mut0. 3 Publications
    VAR_022394
    Natural varianti109 – 1091Q → R in MMAM; mut0. 1 Publication
    VAR_023473
    Natural varianti110 – 1101Y → C in MMAM. 1 Publication
    VAR_075380
    Natural varianti137 – 1371A → G in MMAM. 1 Publication
    VAR_075381
    Natural varianti137 – 1371A → V in MMAM; mut0. 2 Publications
    VAR_022395
    Natural varianti143 – 1431H → Y in MMAM; mut0. 1 Publication
    VAR_075382
    Natural varianti145 – 1451G → S in MMAM; mut0. 1 Publication
    VAR_026598
    Natural varianti148 – 1481S → L in MMAM; mut0. 2 Publications
    VAR_022396
    Natural varianti156 – 1561D → N in MMAM; mut-. 1 Publication
    VAR_022397
    Natural varianti158 – 1581G → V in MMAM; mut0. 1 Publication
    VAR_022398
    Natural varianti174 – 1741F → S in MMAM; mut0. 3 Publications
    VAR_022399
    Natural varianti186 – 1861M → V in MMAM; mut-. 1 Publication
    VAR_026599
    Natural varianti189 – 1891N → K in MMAM; mut-. 1 Publication
    VAR_026600
    Natural varianti191 – 1911A → E in MMAM; mut- and mut0; affects proper folding; reduced protein level. 6 Publications
    VAR_004411
    Natural varianti197 – 1971A → E in MMAM; mut0. 1 Publication
    VAR_026601
    Natural varianti203 – 2031G → R in MMAM; mut0. 4 Publications
    VAR_022400
    Natural varianti215 – 2151G → C in MMAM; mut- and mut0. 1 Publication
    VAR_026602
    Natural varianti215 – 2151G → S in MMAM; mut0. 3 Publications
    VAR_022401
    Natural varianti218 – 2181Q → H in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability. 4 Publications
    VAR_022402
    Natural varianti219 – 2191N → Y in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity. 7 Publications
    VAR_022403
    Natural varianti228 – 2281R → Q in MMAM; mut0. 2 Publications
    VAR_004412
    Natural varianti230 – 2301T → I in MMAM; mut-. 1 Publication
    VAR_026603
    Natural varianti231 – 2311Y → N in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 4 Publications
    VAR_004413
    Natural varianti262 – 2621S → N in MMAM; mut0. 2 Publications
    VAR_022404
    Natural varianti265 – 2651H → Y in MMAM; mut-. 1 Publication
    VAR_026604
    Natural varianti281 – 2811L → S in MMAM; mut0. 1 Publication
    VAR_026605
    Natural varianti288 – 2881S → P in MMAM; mut0. 1 Publication
    VAR_075383
    Natural varianti291 – 2911G → E in MMAM; mut0. 1 Publication
    VAR_026606
    Natural varianti293 – 2931Q → P in MMAM; mut0. 1 Publication
    VAR_022405
    Natural varianti305 – 3051L → S in MMAM; mut0. 2 Publications
    VAR_026607
    Natural varianti306 – 3061S → F in MMAM; mut0. 1 Publication
    VAR_026608
    Natural varianti312 – 3121G → V in MMAM; mut0. 2 Publications
    VAR_004414
    Natural varianti316 – 3161Y → C in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; no decreased affinity for adenosylcob(III)alamin. 2 Publications
    VAR_026609
    Natural varianti324 – 3241A → T in MMAM; mut-. 2 Publications
    VAR_023474
    Natural varianti328 – 3281L → F in MMAM; mut0; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity. 4 Publications
    VAR_022406
    Natural varianti328 – 3281L → P in MMAM; mut0. 1 Publication
    VAR_023475
    Natural varianti344 – 3441S → F in MMAM; mut-; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin. 2 Publications
    VAR_075384
    Natural varianti346 – 3461Missing in MMAM; mut0. 2 Publications
    VAR_004415
    Natural varianti347 – 3471L → R in MMAM; mut0. 1 Publication
    VAR_026610
    Natural varianti350 – 3501H → Y in MMAM; mut0. 1 Publication
    VAR_026611
    Natural varianti364 – 3641Y → S in MMAM. 1 Publication
    VAR_075385
    Natural varianti366 – 3661N → S in MMAM; mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 2 Publications
    VAR_075386
    Natural varianti368 – 3681V → D in MMAM.
    VAR_004416
    Natural varianti369 – 3691R → C in MMAM; mut0. 1 Publication
    VAR_026612
    Natural varianti369 – 3691R → H in MMAM; mut- and mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability. 4 Publications
    VAR_004417
    Natural varianti370 – 3701T → P in MMAM; mut0. 1 Publication
    VAR_026613
    Natural varianti377 – 3771A → E in MMAM; mut0. 2 Publications
    VAR_004418
    Natural varianti383 – 3831Q → H in MMAM; mut0. 1 Publication
    VAR_026614
    Natural varianti383 – 3831Q → P in MMAM; mut0. 1 Publication
    VAR_026615
    Natural varianti386 – 3861H → N in MMAM; mut0. 1 Publication
    VAR_026616
    Natural varianti387 – 3871T → I in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 3 Publications
    VAR_075387
    Natural varianti388 – 3881N → H in MMAM; mut0. 1 Publication
    VAR_026617
    Natural varianti389 – 3891Missing in MMAM; mut0. 1 Publication
    VAR_026618
    Natural varianti412 – 4121Missing in MMAM; mut0. 1 Publication
    VAR_026619
    Natural varianti426 – 4261G → R in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 2 Publications
    VAR_026620
    Natural varianti427 – 4271G → D in MMAM; mut0. 1 Publication
    VAR_026621
    Natural varianti454 – 4541G → E in MMAM; mut0. 2 Publications
    VAR_075388
    Natural varianti514 – 5141Q → E in MMAM; unknown pathological significance. 1 Publication
    VAR_075389
    Natural varianti518 – 5181L → P in MMAM; mut0. 1 Publication
    VAR_026622
    Natural varianti535 – 5351A → P in MMAM; mut0. 1 Publication
    VAR_022408
    Natural varianti560 – 5601C → Y in MMAM; mut0. 1 Publication
    VAR_026623
    Natural varianti566 – 5661T → R in MMAM; mut0. 1 Publication
    VAR_026624
    Natural varianti573 – 5731F → S in MMAM; mut-; affects proper folding; no effect on protein abundance; no decreased of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; does not alter thermodynamic stability. 2 Publications
    VAR_026625
    Natural varianti587 – 5871Y → C in MMAM; mut-. 1 Publication
    VAR_022409
    Natural varianti615 – 6151P → L in MMAM; mut0; affects proper folding; reduced strongly protein level. 2 Publications
    VAR_075390
    Natural varianti615 – 6151P → R in MMAM; mut0. 1 Publication
    VAR_026626
    Natural varianti615 – 6151P → T in MMAM; mut0; affects proper folding; reduced strongly protein level. 4 Publications
    VAR_022410
    Natural varianti616 – 6161R → C in MMAM; mut0. 2 Publications
    VAR_023476
    Natural varianti617 – 6171L → R in MMAM. 1 Publication
    VAR_023477
    Natural varianti621 – 6211K → N in MMAM; mut0. 1 Publication
    VAR_022411
    Natural varianti623 – 6231G → R in MMAM; mut0. 4 Publications
    VAR_004420
    Natural varianti624 – 6241Q → R in MMAM. 1 Publication
    VAR_022412
    Natural varianti625 – 6251D → V in MMAM; unknown pathological significance. 1 Publication
    VAR_075391
    Natural varianti626 – 6261G → C in MMAM; mut-. 1 Publication
    VAR_004421
    Natural varianti627 – 6271H → R in MMAM; mut0. 2 Publications
    VAR_022413
    Natural varianti630 – 6301G → E in MMAM; mut0. 3 Publications
    VAR_004422
    Natural varianti633 – 6331V → G in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; does not alter thermodynamic stability. 4 Publications
    VAR_004423
    Natural varianti637 – 6371G → E in MMAM; mut-. 1 Publication
    VAR_022414
    Natural varianti637 – 6371G → R in MMAM; mut0. 1 Publication
    VAR_026627
    Natural varianti638 – 6381F → I in MMAM; mut0. 1 Publication
    VAR_022415
    Natural varianti640 – 6401D → Y in MMAM; mut0. 1 Publication
    VAR_022416
    Natural varianti642 – 6421G → R in MMAM; mut-. 2 Publications
    VAR_022417
    Natural varianti648 – 6481G → D in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 2 Publications
    VAR_004424
    Natural varianti669 – 6691V → E in MMAM; mut0.
    VAR_004425
    Natural varianti674 – 6741L → F in MMAM; unknown pathological significance. 1 Publication
    VAR_075392
    Natural varianti678 – 6781H → R in MMAM; mut-. 2 Publications
    VAR_004427
    Natural varianti684 – 6841E → EL in MMAM; mut-. 1 Publication
    VAR_004428
    Natural varianti685 – 6851L → R in MMAM; mut-. 2 Publications
    VAR_004429
    Natural varianti692 – 6921L → P in MMAM. 1 Publication
    VAR_075393
    Natural varianti694 – 6941R → L in MMAM; mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 2 Publications
    VAR_075394
    Natural varianti694 – 6941R → W in MMAM; mut- and mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 7 Publications
    VAR_004430
    Natural varianti700 – 7001M → K in MMAM; mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 4 Publications
    VAR_022418
    Natural varianti703 – 7031G → R in MMAM; mut0. 2 Publications
    VAR_004431
    Natural varianti717 – 7171G → V in MMAM; mut-; no effect on protein abundance; interfers with the binding of the cofactor to the apoenzyme; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; decreased thermodynamic stability. 6 Publications
    VAR_004432

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MalaCardsiMUT.
    MIMi251000. phenotype.
    Orphaneti79312. Vitamin B12-unresponsive methylmalonic acidemia type mut-.
    289916. Vitamin B12-unresponsive methylmalonic acidemia type mut0.
    PharmGKBiPA31327.

    Chemistry

    DrugBankiDB00115. Cyanocobalamin.
    DB00200. Hydroxocobalamin.

    Polymorphism and mutation databases

    BioMutaiMUT.
    DMDMi317373575.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3232MitochondrionAdd
    BLAST
    Chaini33 – 750718Methylmalonyl-CoA mutase, mitochondrialPRO_0000019293Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei89 – 891N6-acetyllysineBy similarity
    Modified residuei212 – 2121N6-acetyllysineBy similarity
    Modified residuei335 – 3351N6-acetyllysineBy similarity
    Modified residuei343 – 3431N6-succinyllysineBy similarity
    Modified residuei481 – 4811PhosphoserineCombined sources
    Modified residuei595 – 5951N6-succinyllysineBy similarity
    Modified residuei602 – 6021N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP22033.
    PaxDbiP22033.
    PRIDEiP22033.

    PTM databases

    iPTMnetiP22033.
    PhosphoSiteiP22033.

    Expressioni

    Gene expression databases

    BgeeiP22033.
    CleanExiHS_MUT.
    ExpressionAtlasiP22033. baseline and differential.
    GenevisibleiP22033. HS.

    Organism-specific databases

    HPAiHPA035971.
    HPA035972.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi110680. 13 interactions.
    IntActiP22033. 3 interactions.
    MINTiMINT-3009603.
    STRINGi9606.ENSP00000274813.

    Structurei

    Secondary structure

    1
    750
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 334Combined sources
    Helixi41 – 5010Combined sources
    Turni51 – 533Combined sources
    Helixi56 – 594Combined sources
    Helixi75 – 784Combined sources
    Beta strandi95 – 984Combined sources
    Beta strandi101 – 1033Combined sources
    Beta strandi106 – 1116Combined sources
    Helixi116 – 12813Combined sources
    Beta strandi133 – 1364Combined sources
    Helixi140 – 1434Combined sources
    Helixi151 – 1533Combined sources
    Turni154 – 1596Combined sources
    Beta strandi160 – 1623Combined sources
    Helixi167 – 1737Combined sources
    Turni174 – 1763Combined sources
    Turni179 – 1813Combined sources
    Beta strandi183 – 1864Combined sources
    Helixi192 – 20514Combined sources
    Helixi210 – 2123Combined sources
    Beta strandi214 – 2174Combined sources
    Helixi222 – 2265Combined sources
    Helixi235 – 25218Combined sources
    Beta strandi259 – 2624Combined sources
    Helixi264 – 2696Combined sources
    Helixi273 – 29321Combined sources
    Helixi298 – 3014Combined sources
    Helixi302 – 3043Combined sources
    Beta strandi307 – 3115Combined sources
    Helixi315 – 33723Combined sources
    Helixi342 – 3454Combined sources
    Beta strandi349 – 3535Combined sources
    Beta strandi360 – 3623Combined sources
    Helixi365 – 37915Combined sources
    Beta strandi383 – 3864Combined sources
    Turni390 – 3945Combined sources
    Helixi399 – 41517Combined sources
    Helixi418 – 4203Combined sources
    Beta strandi421 – 4233Combined sources
    Turni424 – 4274Combined sources
    Helixi429 – 45123Combined sources
    Helixi455 – 4617Combined sources
    Helixi463 – 48119Combined sources
    Beta strandi482 – 4843Combined sources
    Turni487 – 4893Combined sources
    Beta strandi490 – 4923Combined sources
    Helixi508 – 52417Combined sources
    Helixi527 – 54317Combined sources
    Helixi548 – 55710Combined sources
    Helixi562 – 57312Combined sources
    Helixi586 – 5916Combined sources
    Helixi595 – 61117Combined sources
    Beta strandi616 – 6205Combined sources
    Helixi629 – 64012Combined sources
    Beta strandi644 – 6474Combined sources
    Helixi654 – 66310Combined sources
    Beta strandi667 – 6737Combined sources
    Helixi678 – 69114Combined sources
    Beta strandi697 – 7048Combined sources
    Helixi707 – 7093Combined sources
    Helixi710 – 7167Combined sources
    Beta strandi720 – 7223Combined sources
    Helixi728 – 74417Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XIJX-ray1.95A12-750[»]
    2XIQX-ray1.95A/B12-750[»]
    3BICX-ray2.60A/B12-750[»]
    ProteinModelPortaliP22033.
    SMRiP22033. Positions 36-749.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22033.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini614 – 746133B12-bindingPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the methylmalonyl-CoA mutase family.Curated
    Contains 1 B12-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiENOG410IE7I. Eukaryota.
    COG1884. LUCA.
    COG2185. LUCA.
    GeneTreeiENSGT00390000011892.
    HOGENOMiHOG000003917.
    HOVERGENiHBG006423.
    InParanoidiP22033.
    KOiK01847.
    OMAiGVNKYRP.
    OrthoDBiEOG78PV8G.
    PhylomeDBiP22033.
    TreeFamiTF313557.

    Family and domain databases

    Gene3Di3.20.20.240. 1 hit.
    3.40.50.280. 1 hit.
    InterProiIPR006159. 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]
    PfamiPF02310. B12-binding. 1 hit.
    PF01642. MM_CoA_mutase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51703. SSF51703. 1 hit.
    SSF52242. SSF52242. 1 hit.
    TIGRFAMsiTIGR00640. acid_CoA_mut_C. 1 hit.
    TIGR00641. acid_CoA_mut_N. 1 hit.
    PROSITEiPS51332. B12_BINDING. 1 hit.
    PS00544. METMALONYL_COA_MUTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P22033-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLRAKNQLFL LSPHYLRQVK ESSGSRLIQQ RLLHQQQPLH PEWAALAKKQ
    60 70 80 90 100
    LKGKNPEDLI WHTPEGISIK PLYSKRDTMD LPEELPGVKP FTRGPYPTMY
    110 120 130 140 150
    TFRPWTIRQY AGFSTVEESN KFYKDNIKAG QQGLSVAFDL ATHRGYDSDN
    160 170 180 190 200
    PRVRGDVGMA GVAIDTVEDT KILFDGIPLE KMSVSMTMNG AVIPVLANFI
    210 220 230 240 250
    VTGEEQGVPK EKLTGTIQND ILKEFMVRNT YIFPPEPSMK IIADIFEYTA
    260 270 280 290 300
    KHMPKFNSIS ISGYHMQEAG ADAILELAYT LADGLEYSRT GLQAGLTIDE
    310 320 330 340 350
    FAPRLSFFWG IGMNFYMEIA KMRAGRRLWA HLIEKMFQPK NSKSLLLRAH
    360 370 380 390 400
    CQTSGWSLTE QDPYNNIVRT AIEAMAAVFG GTQSLHTNSF DEALGLPTVK
    410 420 430 440 450
    SARIARNTQI IIQEESGIPK VADPWGGSYM MECLTNDVYD AALKLINEIE
    460 470 480 490 500
    EMGGMAKAVA EGIPKLRIEE CAARRQARID SGSEVIVGVN KYQLEKEDAV
    510 520 530 540 550
    EVLAIDNTSV RNRQIEKLKK IKSSRDQALA ERCLAALTEC AASGDGNILA
    560 570 580 590 600
    LAVDASRARC TVGEITDALK KVFGEHKAND RMVSGAYRQE FGESKEITSA
    610 620 630 640 650
    IKRVHKFMER EGRRPRLLVA KMGQDGHDRG AKVIATGFAD LGFDVDIGPL
    660 670 680 690 700
    FQTPREVAQQ AVDADVHAVG ISTLAAGHKT LVPELIKELN SLGRPDILVM
    710 720 730 740 750
    CGGVIPPQDY EFLFEVGVSN VFGPGTRIPK AAVQVLDDIE KCLEKKQQSV
    Length:750
    Mass (Da):83,134
    Last modified:January 11, 2011 - v4
    Checksum:iB5909729C08B562F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531V → L in AAA99226 (PubMed:1980486).Curated
    Sequence conflicti236 – 2361E → D in AAA99226 (PubMed:1980486).Curated
    Sequence conflicti274 – 2774ILEL → FWSW in AAA99226 (PubMed:1980486).Curated
    Sequence conflicti316 – 3161Y → H in AAA99226 (PubMed:1980486).Curated
    Sequence conflicti505 – 5051I → T in AAA99226 (PubMed:1980486).Curated
    Sequence conflicti516 – 5161E → G in AAA99226 (PubMed:1980486).Curated
    Sequence conflicti591 – 5911F → Y in AAA99226 (PubMed:1980486).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti69 – 691I → V.2 Publications
    Corresponds to variant rs115923556 [ dbSNP | Ensembl ].
    VAR_023472
    Natural varianti86 – 861P → L in MMAM; mut0 and mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 2 Publications
    VAR_026592
    Natural varianti87 – 871G → E in MMAM; mut0. 1 Publication
    VAR_026593
    Natural varianti93 – 931R → H in MMAM; mut0. 3 Publications
    Corresponds to variant rs121918251 [ dbSNP | Ensembl ].
    VAR_004409
    Natural varianti94 – 941G → R in MMAM; mut0. 1 Publication
    VAR_026594
    Natural varianti94 – 941G → V in MMAM; mut- and mut0. 2 Publications
    VAR_022393
    Natural varianti95 – 951P → R in MMAM; mut0. 1 Publication
    VAR_026595
    Natural varianti100 – 1001Y → C in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 2 Publications
    VAR_075379
    Natural varianti105 – 1051W → R in MMAM; mut0. 2 Publications
    VAR_004410
    Natural varianti108 – 1081R → C in MMAM; mut0. 2 Publications
    Corresponds to variant rs121918257 [ dbSNP | Ensembl ].
    VAR_026596
    Natural varianti108 – 1081R → G in MMAM; mut-. 1 Publication
    VAR_026597
    Natural varianti108 – 1081R → H in MMAM; mut0. 3 Publications
    VAR_022394
    Natural varianti109 – 1091Q → R in MMAM; mut0. 1 Publication
    VAR_023473
    Natural varianti110 – 1101Y → C in MMAM. 1 Publication
    VAR_075380
    Natural varianti137 – 1371A → G in MMAM. 1 Publication
    VAR_075381
    Natural varianti137 – 1371A → V in MMAM; mut0. 2 Publications
    VAR_022395
    Natural varianti143 – 1431H → Y in MMAM; mut0. 1 Publication
    VAR_075382
    Natural varianti145 – 1451G → S in MMAM; mut0. 1 Publication
    VAR_026598
    Natural varianti148 – 1481S → L in MMAM; mut0. 2 Publications
    VAR_022396
    Natural varianti156 – 1561D → N in MMAM; mut-. 1 Publication
    VAR_022397
    Natural varianti158 – 1581G → V in MMAM; mut0. 1 Publication
    VAR_022398
    Natural varianti174 – 1741F → S in MMAM; mut0. 3 Publications
    VAR_022399
    Natural varianti186 – 1861M → V in MMAM; mut-. 1 Publication
    VAR_026599
    Natural varianti189 – 1891N → K in MMAM; mut-. 1 Publication
    VAR_026600
    Natural varianti191 – 1911A → E in MMAM; mut- and mut0; affects proper folding; reduced protein level. 6 Publications
    VAR_004411
    Natural varianti197 – 1971A → E in MMAM; mut0. 1 Publication
    VAR_026601
    Natural varianti203 – 2031G → R in MMAM; mut0. 4 Publications
    VAR_022400
    Natural varianti215 – 2151G → C in MMAM; mut- and mut0. 1 Publication
    VAR_026602
    Natural varianti215 – 2151G → S in MMAM; mut0. 3 Publications
    VAR_022401
    Natural varianti218 – 2181Q → H in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability. 4 Publications
    VAR_022402
    Natural varianti219 – 2191N → Y in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity. 7 Publications
    VAR_022403
    Natural varianti228 – 2281R → Q in MMAM; mut0. 2 Publications
    VAR_004412
    Natural varianti230 – 2301T → I in MMAM; mut-. 1 Publication
    VAR_026603
    Natural varianti231 – 2311Y → N in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability. 4 Publications
    VAR_004413
    Natural varianti262 – 2621S → N in MMAM; mut0. 2 Publications
    VAR_022404
    Natural varianti265 – 2651H → Y in MMAM; mut-. 1 Publication
    VAR_026604
    Natural varianti281 – 2811L → S in MMAM; mut0. 1 Publication
    VAR_026605
    Natural varianti288 – 2881S → P in MMAM; mut0. 1 Publication
    VAR_075383
    Natural varianti291 – 2911G → E in MMAM; mut0. 1 Publication
    VAR_026606
    Natural varianti293 – 2931Q → P in MMAM; mut0. 1 Publication
    VAR_022405
    Natural varianti305 – 3051L → S in MMAM; mut0. 2 Publications
    VAR_026607
    Natural varianti306 – 3061S → F in MMAM; mut0. 1 Publication
    VAR_026608
    Natural varianti312 – 3121G → V in MMAM; mut0. 2 Publications
    VAR_004414
    Natural varianti316 – 3161Y → C in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; no decreased affinity for adenosylcob(III)alamin. 2 Publications
    VAR_026609
    Natural varianti324 – 3241A → T in MMAM; mut-. 2 Publications
    VAR_023474
    Natural varianti328 – 3281L → F in MMAM; mut0; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity. 4 Publications