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Protein

Methylmalonyl-CoA mutase small subunit

Gene

mutA

Organism
Propionibacterium freudenreichii subsp. shermanii
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.

Catalytic activityi

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

Cofactori

Pathwayi: propanoyl-CoA degradation

This protein is involved in step 3 of the subpathway that synthesizes succinyl-CoA from propanoyl-CoA.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. Methylmalonyl-CoA mutase large subunit (mutB), Methylmalonyl-CoA mutase small subunit (mutA)
This subpathway is part of the pathway propanoyl-CoA degradation, which is itself part of Metabolic intermediate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinyl-CoA from propanoyl-CoA, the pathway propanoyl-CoA degradation and in Metabolic intermediate metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalamin, Cobalt

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13076.
BRENDAi5.4.99.2. 5032.
SABIO-RKP11652.
UniPathwayiUPA00945; UER00910.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylmalonyl-CoA mutase small subunit (EC:5.4.99.2)
Alternative name(s):
MCB-beta
Gene namesi
Name:mutA
OrganismiPropionibacterium freudenreichii subsp. shermanii
Taxonomic identifieri1752 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPropionibacterialesPropionibacteriaceaePropionibacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 638637Methylmalonyl-CoA mutase small subunitPRO_0000194268Add
BLAST

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Binary interactionsi

WithEntry#Exp.IntActNotes
mutBP116534EBI-1027328,EBI-1027336

Protein-protein interaction databases

DIPiDIP-6149N.
IntActiP11652. 1 interaction.
MINTiMINT-1536026.
STRINGi754252.PFREUD_07660.

Structurei

Secondary structure

1
638
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 263Combined sources
Helixi32 – 4413Combined sources
Beta strandi49 – 513Combined sources
Helixi55 – 628Combined sources
Helixi78 – 803Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi107 – 1137Combined sources
Helixi118 – 12912Combined sources
Turni130 – 1323Combined sources
Beta strandi135 – 1417Combined sources
Turni147 – 1493Combined sources
Helixi150 – 1534Combined sources
Turni154 – 1563Combined sources
Turni159 – 1613Combined sources
Beta strandi163 – 1675Combined sources
Helixi172 – 18413Combined sources
Beta strandi186 – 1883Combined sources
Helixi190 – 1923Combined sources
Beta strandi195 – 1995Combined sources
Helixi201 – 2088Combined sources
Helixi214 – 2163Combined sources
Helixi217 – 2237Combined sources
Beta strandi225 – 2273Combined sources
Beta strandi232 – 2376Combined sources
Helixi239 – 2424Combined sources
Turni243 – 2453Combined sources
Helixi248 – 26821Combined sources
Helixi273 – 2775Combined sources
Beta strandi280 – 2867Combined sources
Helixi290 – 31122Combined sources
Helixi315 – 3173Combined sources
Beta strandi322 – 3265Combined sources
Helixi328 – 3303Combined sources
Beta strandi333 – 3353Combined sources
Helixi338 – 35316Combined sources
Beta strandi356 – 3594Combined sources
Turni363 – 3675Combined sources
Beta strandi369 – 3735Combined sources
Helixi374 – 38815Combined sources
Beta strandi394 – 3963Combined sources
Turni398 – 4014Combined sources
Helixi403 – 42523Combined sources
Helixi429 – 4346Combined sources
Helixi437 – 45418Combined sources
Turni461 – 4633Combined sources
Beta strandi464 – 4663Combined sources
Helixi495 – 50612Combined sources
Beta strandi507 – 5093Combined sources
Beta strandi514 – 5174Combined sources
Helixi521 – 53717Combined sources
Beta strandi544 – 5463Combined sources
Helixi550 – 56011Combined sources
Beta strandi563 – 5686Combined sources
Helixi571 – 58717Combined sources
Beta strandi591 – 5977Combined sources
Helixi599 – 6057Combined sources
Helixi606 – 6127Combined sources
Beta strandi615 – 6173Combined sources
Helixi623 – 63311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E1CX-ray2.62B/D2-638[»]
1REQX-ray2.00B/D2-638[»]
2REQX-ray2.50B/D2-638[»]
3REQX-ray2.70B2-638[»]
4REQX-ray2.20B/D2-638[»]
5REQX-ray2.20B/D2-638[»]
6REQX-ray2.20B/D2-638[»]
7REQX-ray2.20B/D2-638[»]
ProteinModelPortaliP11652.
SMRiP11652. Positions 16-638.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11652.

Family & Domainsi

Sequence similaritiesi

Belongs to the methylmalonyl-CoA mutase family.Curated

Phylogenomic databases

eggNOGiENOG4105CMN. Bacteria.
COG1884. LUCA.

Family and domain databases

Gene3Di1.10.196.20. 1 hit.
3.20.20.240. 1 hit.
3.40.50.280. 1 hit.
InterProiIPR016176. Cbl-dep_enz_cat.
IPR014348. Cbl-dep_enz_cat-sub.
IPR006158. Cobalamin-bd.
IPR024067. Me-malonyl-CoA_mutase_sm_su_N.
IPR006099. MeMalonylCoA_mutase_a/b_cat.
IPR004608. MMCoA_mutase_b.
[Graphical view]
PfamiPF01642. MM_CoA_mutase. 1 hit.
[Graphical view]
SUPFAMiSSF51703. SSF51703. 1 hit.
SSF52242. SSF52242. 1 hit.
TIGRFAMsiTIGR00642. mmCoA_mut_beta. 1 hit.
PROSITEiPS00544. METMALONYL_COA_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P11652-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSTDQGTNP ADTDDLTPTT LSLAGDFPKA TEEQWEREVE KVLNRGRPPE
60 70 80 90 100
KQLTFAECLK RLTVHTVDGI DIVPMYRPKD APKKLGYPGV APFTRGTTVR
110 120 130 140 150
NGDMDAWDVR ALHEDPDEKF TRKAILEGLE RGVTSLLLRV DPDAIAPEHL
160 170 180 190 200
DEVLSDVLLE MTKVEVFSRY DQGAAAEALV SVYERSDKPA KDLALNLGLD
210 220 230 240 250
PIAFAALQGT EPDLTVLGDW VRRLAKFSPD SRAVTIDANI YHNAGAGDVA
260 270 280 290 300
ELAWALATGA EYVRALVEQG FTATEAFDTI NFRVTATHDQ FLTIARLRAL
310 320 330 340 350
REAWARIGEV FGVDEDKRGA RQNAITSWRD VTREDPYVNI LRGSIATFSA
360 370 380 390 400
SVGGAESITT LPFTQALGLP EDDFPLRIAR NTGIVLAEEV NIGRVNDPAG
410 420 430 440 450
GSYYVESLTR SLADAAWKEF QEVEKLGGMS KAVMTEHVTK VLDACNAERA
460 470 480 490 500
KRLANRKQPI TAVSEFPMIG ARSIETKPFP AAPARKGLAW HRDSEVFEQL
510 520 530 540 550
MDRSTSVSER PKVFLACLGT RRDFGGREGF SSPVWHIAGI DTPQVEGGTT
560 570 580 590 600
AEIVEAFKKS GAQVADLCSS AKVYAQQGLE VAKALKAAGA KALYLSGAFK
610 620 630
EFGDDAAEAE KLIDGRLFMG MDVVDTLSST LDILGVAK
Length:638
Mass (Da):69,464
Last modified:January 23, 2007 - v3
Checksum:iF44C708AA8D47075
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14965 Genomic DNA. Translation: CAA33089.1.
PIRiS04640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14965 Genomic DNA. Translation: CAA33089.1.
PIRiS04640.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E1CX-ray2.62B/D2-638[»]
1REQX-ray2.00B/D2-638[»]
2REQX-ray2.50B/D2-638[»]
3REQX-ray2.70B2-638[»]
4REQX-ray2.20B/D2-638[»]
5REQX-ray2.20B/D2-638[»]
6REQX-ray2.20B/D2-638[»]
7REQX-ray2.20B/D2-638[»]
ProteinModelPortaliP11652.
SMRiP11652. Positions 16-638.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6149N.
IntActiP11652. 1 interaction.
MINTiMINT-1536026.
STRINGi754252.PFREUD_07660.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CMN. Bacteria.
COG1884. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00945; UER00910.
BioCyciMetaCyc:MONOMER-13076.
BRENDAi5.4.99.2. 5032.
SABIO-RKP11652.

Miscellaneous databases

EvolutionaryTraceiP11652.

Family and domain databases

Gene3Di1.10.196.20. 1 hit.
3.20.20.240. 1 hit.
3.40.50.280. 1 hit.
InterProiIPR016176. Cbl-dep_enz_cat.
IPR014348. Cbl-dep_enz_cat-sub.
IPR006158. Cobalamin-bd.
IPR024067. Me-malonyl-CoA_mutase_sm_su_N.
IPR006099. MeMalonylCoA_mutase_a/b_cat.
IPR004608. MMCoA_mutase_b.
[Graphical view]
PfamiPF01642. MM_CoA_mutase. 1 hit.
[Graphical view]
SUPFAMiSSF51703. SSF51703. 1 hit.
SSF52242. SSF52242. 1 hit.
TIGRFAMsiTIGR00642. mmCoA_mut_beta. 1 hit.
PROSITEiPS00544. METMALONYL_COA_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and structural characterization of the genes coding for adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii."
    Marsh E.N., McKie N., Davis N.K., Leadlay P.F.
    Biochem. J. 260:345-352(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 4-9; 96-100; 302-306; 473-478 AND 523-527.
    Strain: NCIB 9885.
  2. "Methylmalonyl-CoA mutase from Propionibacterium shermanii. Evidence for the presence of two masked cysteine residues."
    Marsh E.N., Leadlay P.F.
    Biochem. J. 260:339-343(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 515-518.
    Strain: NCIB 9885.
  3. "How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2-A resolution."
    Mancia F., Keep N.H., Nakagawa A., Leadlay P.F., McSweeney S., Rasmussen B., Bosecke P., Diat O., Evans P.R.
    Structure 4:339-350(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    Strain: NCIB 9885.
  4. "Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism."
    Mancia F., Evans P.R.
    Structure 6:711-720(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    Strain: NCIB 9885.

Entry informationi

Entry nameiMUTA_PROFR
AccessioniPrimary (citable) accession number: P11652
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.