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P22033

- MUTA_HUMAN

UniProt

P22033 - MUTA_HUMAN

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Protein

Methylmalonyl-CoA mutase, mitochondrial

Gene
MUT
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

Cofactori

Adenosylcobalamin.

Sites

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

GO - Molecular functioni

  1. cobalamin binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. methylmalonyl-CoA mutase activity Source: ProtInc
  4. modified amino acid binding Source: UniProtKB

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. cobalamin metabolic process Source: Reactome
  3. fatty acid beta-oxidation Source: Reactome
  4. homocysteine metabolic process Source: UniProtKB
  5. post-embryonic development Source: Ensembl
  6. short-chain fatty acid catabolic process Source: Reactome
  7. small molecule metabolic process Source: Reactome
  8. vitamin metabolic process Source: Reactome
  9. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalamin, Cobalt, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS07322-MONOMER.
ReactomeiREACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_169313. Defective MUT causes methylmalonic aciduria mut type.
REACT_169316. Defective MMAA causes methylmalonic aciduria type cblA.
REACT_993. Propionyl-CoA catabolism.
SABIO-RKP22033.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylmalonyl-CoA mutase, mitochondrial (EC:5.4.99.2)
Short name:
MCM
Alternative name(s):
Methylmalonyl-CoA isomerase
Gene namesi
Name:MUT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:7526. MUT.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrion Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

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.14 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti86 – 861P → L in MMAM; mut0. 1 Publication
VAR_026592
Natural varianti87 – 871G → E in MMAM; mut0. 1 Publication
VAR_026593
Natural varianti93 – 931R → H in MMAM; mut0. 2 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 varianti105 – 1051W → R in MMAM; mut0. 2 Publications
VAR_004410
Natural varianti108 – 1081R → C in MMAM; mut0. 1 Publication
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. 2 Publications
VAR_022394
Natural varianti109 – 1091Q → R in MMAM; mut0. 1 Publication
VAR_023473
Natural varianti137 – 1371A → V in MMAM; mut0. 1 Publication
VAR_022395
Natural varianti145 – 1451G → S in MMAM; mut0. 1 Publication
VAR_026598
Natural varianti148 – 1481S → L in MMAM. 1 Publication
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. 2 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. 4 Publications
VAR_004411
Natural varianti197 – 1971A → E in MMAM; mut0. 1 Publication
VAR_026601
Natural varianti203 – 2031G → R in MMAM; mut0. 3 Publications
VAR_022400
Natural varianti215 – 2151G → C in MMAM; mut- and mut0. 1 Publication
VAR_026602
Natural varianti215 – 2151G → S in MMAM; mut0. 2 Publications
VAR_022401
Natural varianti218 – 2181Q → H in MMAM; mut0. 2 Publications
VAR_022402
Natural varianti219 – 2191N → Y in MMAM; mut0. 4 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-. 2 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 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. 1 Publication
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-. 1 Publication
VAR_026609
Natural varianti324 – 3241A → T in MMAM; mut-. 2 Publications
VAR_023474
Natural varianti328 – 3281L → F in MMAM; mut0. 1 Publication
VAR_022406
Natural varianti328 – 3281L → P in MMAM; mut0. 1 Publication
VAR_023475
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 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. 2 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 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-. 1 Publication
VAR_026620
Natural varianti427 – 4271G → D in MMAM; mut0. 1 Publication
VAR_026621
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-. 1 Publication
VAR_026625
Natural varianti587 – 5871Y → C in MMAM; mut-. 1 Publication
VAR_022409
Natural varianti615 – 6151P → R in MMAM; mut0. 1 Publication
VAR_026626
Natural varianti615 – 6151P → T in MMAM; mut0. 1 Publication
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 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. 2 Publications
VAR_004422
Natural varianti633 – 6331V → G in MMAM; mut-. 2 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-. 1 Publication
VAR_004424
Natural varianti669 – 6691V → E in MMAM; mut0.
VAR_004425
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 varianti694 – 6941R → W in MMAM; mut- and mut0. 4 Publications
VAR_004430
Natural varianti700 – 7001M → K in MMAM; mut-. 2 Publications
VAR_022418
Natural varianti703 – 7031G → R in MMAM; mut0. 2 Publications
VAR_004431
Natural varianti717 – 7171G → V in MMAM; mut-; interfers with the binding of the cofactor to the apoenzyme. 5 Publications
VAR_004432

Keywords - Diseasei

Disease mutation

Organism-specific databases

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

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-acetyllysine By similarity
Modified residuei212 – 2121N6-acetyllysine By similarity
Modified residuei335 – 3351N6-acetyllysine By similarity
Modified residuei343 – 3431N6-succinyllysine By similarity
Modified residuei595 – 5951N6-succinyllysine By similarity
Modified residuei602 – 6021N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP22033.
PaxDbiP22033.
PRIDEiP22033.

PTM databases

PhosphoSiteiP22033.

Expressioni

Gene expression databases

BgeeiP22033.
CleanExiHS_MUT.
GenevestigatoriP22033.

Organism-specific databases

HPAiHPA035971.
HPA035972.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi110680. 3 interactions.
IntActiP22033. 2 interactions.
MINTiMINT-3009603.
STRINGi9606.ENSP00000274813.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP22033.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini614 – 746133B12-bindingAdd
BLAST

Sequence similaritiesi

Contains 1 B12-binding domain.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2185.
HOGENOMiHOG000003917.
HOVERGENiHBG006423.
InParanoidiP22033.
KOiK01847.
OMAiMGGMMKA.
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

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MLRAKNQLFL LSPHYLRQVK ESSGSRLIQQ RLLHQQQPLH PEWAALAKKQ    50
LKGKNPEDLI WHTPEGISIK PLYSKRDTMD LPEELPGVKP FTRGPYPTMY 100
TFRPWTIRQY AGFSTVEESN KFYKDNIKAG QQGLSVAFDL ATHRGYDSDN 150
PRVRGDVGMA GVAIDTVEDT KILFDGIPLE KMSVSMTMNG AVIPVLANFI 200
VTGEEQGVPK EKLTGTIQND ILKEFMVRNT YIFPPEPSMK IIADIFEYTA 250
KHMPKFNSIS ISGYHMQEAG ADAILELAYT LADGLEYSRT GLQAGLTIDE 300
FAPRLSFFWG IGMNFYMEIA KMRAGRRLWA HLIEKMFQPK NSKSLLLRAH 350
CQTSGWSLTE QDPYNNIVRT AIEAMAAVFG GTQSLHTNSF DEALGLPTVK 400
SARIARNTQI IIQEESGIPK VADPWGGSYM MECLTNDVYD AALKLINEIE 450
EMGGMAKAVA EGIPKLRIEE CAARRQARID SGSEVIVGVN KYQLEKEDAV 500
EVLAIDNTSV RNRQIEKLKK IKSSRDQALA ERCLAALTEC AASGDGNILA 550
LAVDASRARC TVGEITDALK KVFGEHKAND RMVSGAYRQE FGESKEITSA 600
IKRVHKFMER EGRRPRLLVA KMGQDGHDRG AKVIATGFAD LGFDVDIGPL 650
FQTPREVAQQ AVDADVHAVG ISTLAAGHKT LVPELIKELN SLGRPDILVM 700
CGGVIPPQDY EFLFEVGVSN VFGPGTRIPK AAVQVLDDIE KCLEKKQQSV 750
Length:750
Mass (Da):83,134
Last modified:January 11, 2011 - v4
Checksum:iB5909729C08B562F
GO

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. 1 Publication
VAR_026592
Natural varianti87 – 871G → E in MMAM; mut0. 1 Publication
VAR_026593
Natural varianti93 – 931R → H in MMAM; mut0. 2 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 varianti105 – 1051W → R in MMAM; mut0. 2 Publications
VAR_004410
Natural varianti108 – 1081R → C in MMAM; mut0. 1 Publication
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. 2 Publications
VAR_022394
Natural varianti109 – 1091Q → R in MMAM; mut0. 1 Publication
VAR_023473
Natural varianti137 – 1371A → V in MMAM; mut0. 1 Publication
VAR_022395
Natural varianti145 – 1451G → S in MMAM; mut0. 1 Publication
VAR_026598
Natural varianti148 – 1481S → L in MMAM. 1 Publication
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. 2 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. 4 Publications
VAR_004411
Natural varianti197 – 1971A → E in MMAM; mut0. 1 Publication
VAR_026601
Natural varianti203 – 2031G → R in MMAM; mut0. 3 Publications
VAR_022400
Natural varianti215 – 2151G → C in MMAM; mut- and mut0. 1 Publication
VAR_026602
Natural varianti215 – 2151G → S in MMAM; mut0. 2 Publications
VAR_022401
Natural varianti218 – 2181Q → H in MMAM; mut0. 2 Publications
VAR_022402
Natural varianti219 – 2191N → Y in MMAM; mut0. 4 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-. 2 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 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. 1 Publication
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-. 1 Publication
VAR_026609
Natural varianti324 – 3241A → T in MMAM; mut-. 2 Publications
VAR_023474
Natural varianti328 – 3281L → F in MMAM; mut0. 1 Publication
VAR_022406
Natural varianti328 – 3281L → P in MMAM; mut0. 1 Publication
VAR_023475
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 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. 2 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 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-. 1 Publication
VAR_026620
Natural varianti427 – 4271G → D in MMAM; mut0. 1 Publication
VAR_026621
Natural varianti499 – 4991A → T.4 Publications
Corresponds to variant rs2229385 [ dbSNP | Ensembl ].
VAR_022407
Natural varianti518 – 5181L → P in MMAM; mut0. 1 Publication
VAR_026622
Natural varianti532 – 5321R → H.4 Publications
Corresponds to variant rs1141321 [ dbSNP | Ensembl ].
VAR_004419
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-. 1 Publication
VAR_026625
Natural varianti587 – 5871Y → C in MMAM; mut-. 1 Publication
VAR_022409
Natural varianti598 – 5981T → A.
Corresponds to variant rs9473556 [ dbSNP | Ensembl ].
VAR_030495
Natural varianti615 – 6151P → R in MMAM; mut0. 1 Publication
VAR_026626
Natural varianti615 – 6151P → T in MMAM; mut0. 1 Publication
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 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. 2 Publications
VAR_004422
Natural varianti633 – 6331V → G in MMAM; mut-. 2 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-. 1 Publication
VAR_004424
Natural varianti669 – 6691V → E in MMAM; mut0.
VAR_004425
Natural varianti671 – 6711I → V.11 Publications
Corresponds to variant rs8589 [ dbSNP | Ensembl ].
VAR_004426
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 varianti694 – 6941R → W in MMAM; mut- and mut0. 4 Publications
VAR_004430
Natural varianti700 – 7001M → K in MMAM; mut-. 2 Publications
VAR_022418
Natural varianti703 – 7031G → R in MMAM; mut0. 2 Publications
VAR_004431
Natural varianti717 – 7171G → V in MMAM; mut-; interfers with the binding of the cofactor to the apoenzyme. 5 Publications
VAR_004432

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531V → L in AAA99226. 1 Publication
Sequence conflicti236 – 2361E → D in AAA99226. 1 Publication
Sequence conflicti274 – 2774ILEL → FWSW in AAA99226. 1 Publication
Sequence conflicti316 – 3161Y → H in AAA99226. 1 Publication
Sequence conflicti505 – 5051I → T in AAA99226. 1 Publication
Sequence conflicti516 – 5161E → G in AAA99226. 1 Publication
Sequence conflicti591 – 5911F → Y in AAA99226. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M65131 mRNA. Translation: AAA59569.1.
M37510
, 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.
CCDSiCCDS4924.1.
PIRiA59145.
RefSeqiNP_000246.2. NM_000255.3.
XP_005249200.1. XM_005249143.2.
UniGeneiHs.485527.

Genome annotation databases

EnsembliENST00000274813; ENSP00000274813; ENSG00000146085.
GeneIDi4594.
KEGGihsa:4594.
UCSCiuc003ozg.4. human.

Polymorphism databases

DMDMi317373575.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Methylmalonyl coenzyme A mutase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M65131 mRNA. Translation: AAA59569.1 .
M37510
, 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 .
CCDSi CCDS4924.1.
PIRi A59145.
RefSeqi NP_000246.2. NM_000255.3.
XP_005249200.1. XM_005249143.2.
UniGenei Hs.485527.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XIJ X-ray 1.95 A 12-750 [» ]
2XIQ X-ray 1.95 A/B 12-750 [» ]
3BIC X-ray 2.60 A/B 12-750 [» ]
ProteinModelPortali P22033.
SMRi P22033. Positions 36-749.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110680. 3 interactions.
IntActi P22033. 2 interactions.
MINTi MINT-3009603.
STRINGi 9606.ENSP00000274813.

Chemistry

DrugBanki DB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.

PTM databases

PhosphoSitei P22033.

Polymorphism databases

DMDMi 317373575.

Proteomic databases

MaxQBi P22033.
PaxDbi P22033.
PRIDEi P22033.

Protocols and materials databases

DNASUi 4594.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000274813 ; ENSP00000274813 ; ENSG00000146085 .
GeneIDi 4594.
KEGGi hsa:4594.
UCSCi uc003ozg.4. human.

Organism-specific databases

CTDi 4594.
GeneCardsi GC06M049445.
GeneReviewsi MUT.
H-InvDB HIX0005945.
HGNCi HGNC:7526. MUT.
HPAi HPA035971.
HPA035972.
MIMi 251000. phenotype.
609058. gene.
neXtProti NX_P22033.
Orphaneti 79312. Vitamin B12-unresponsive methylmalonic acidemia type mut-.
289916. Vitamin B12-unresponsive methylmalonic acidemia type mut0.
PharmGKBi PA31327.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2185.
HOGENOMi HOG000003917.
HOVERGENi HBG006423.
InParanoidi P22033.
KOi K01847.
OMAi MGGMMKA.
OrthoDBi EOG78PV8G.
PhylomeDBi P22033.
TreeFami TF313557.

Enzyme and pathway databases

BioCyci MetaCyc:HS07322-MONOMER.
Reactomei REACT_163862. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_169313. Defective MUT causes methylmalonic aciduria mut type.
REACT_169316. Defective MMAA causes methylmalonic aciduria type cblA.
REACT_993. Propionyl-CoA catabolism.
SABIO-RK P22033.

Miscellaneous databases

EvolutionaryTracei P22033.
GeneWikii Methylmalonyl-CoA_mutase.
GenomeRNAii 4594.
NextBioi 17660.
PROi P22033.
SOURCEi Search...

Gene expression databases

Bgeei P22033.
CleanExi HS_MUT.
Genevestigatori P22033.

Family and domain databases

Gene3Di 3.20.20.240. 1 hit.
3.40.50.280. 1 hit.
InterProi IPR006159. 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 ]
Pfami PF02310. B12-binding. 1 hit.
PF01642. MM_CoA_mutase. 1 hit.
[Graphical view ]
SUPFAMi SSF51703. SSF51703. 1 hit.
SSF52242. SSF52242. 1 hit.
TIGRFAMsi TIGR00640. acid_CoA_mut_C. 1 hit.
TIGR00641. acid_CoA_mut_N. 1 hit.
PROSITEi PS51332. B12_BINDING. 1 hit.
PS00544. METMALONYL_COA_MUTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.,