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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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001942682 – 638Methylmalonyl-CoA mutase small subunitAdd BLAST637

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 interactor.
MINTiMINT-1536026.
STRINGi754252.PFREUD_07660.

Structurei

Secondary structure

1638
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi24 – 26Combined sources3
Helixi32 – 44Combined sources13
Beta strandi49 – 51Combined sources3
Helixi55 – 62Combined sources8
Helixi78 – 80Combined sources3
Beta strandi102 – 104Combined sources3
Beta strandi107 – 113Combined sources7
Helixi118 – 129Combined sources12
Turni130 – 132Combined sources3
Beta strandi135 – 141Combined sources7
Turni147 – 149Combined sources3
Helixi150 – 153Combined sources4
Turni154 – 156Combined sources3
Turni159 – 161Combined sources3
Beta strandi163 – 167Combined sources5
Helixi172 – 184Combined sources13
Beta strandi186 – 188Combined sources3
Helixi190 – 192Combined sources3
Beta strandi195 – 199Combined sources5
Helixi201 – 208Combined sources8
Helixi214 – 216Combined sources3
Helixi217 – 223Combined sources7
Beta strandi225 – 227Combined sources3
Beta strandi232 – 237Combined sources6
Helixi239 – 242Combined sources4
Turni243 – 245Combined sources3
Helixi248 – 268Combined sources21
Helixi273 – 277Combined sources5
Beta strandi280 – 286Combined sources7
Helixi290 – 311Combined sources22
Helixi315 – 317Combined sources3
Beta strandi322 – 326Combined sources5
Helixi328 – 330Combined sources3
Beta strandi333 – 335Combined sources3
Helixi338 – 353Combined sources16
Beta strandi356 – 359Combined sources4
Turni363 – 367Combined sources5
Beta strandi369 – 373Combined sources5
Helixi374 – 388Combined sources15
Beta strandi394 – 396Combined sources3
Turni398 – 401Combined sources4
Helixi403 – 425Combined sources23
Helixi429 – 434Combined sources6
Helixi437 – 454Combined sources18
Turni461 – 463Combined sources3
Beta strandi464 – 466Combined sources3
Helixi495 – 506Combined sources12
Beta strandi507 – 509Combined sources3
Beta strandi514 – 517Combined sources4
Helixi521 – 537Combined sources17
Beta strandi544 – 546Combined sources3
Helixi550 – 560Combined sources11
Beta strandi563 – 568Combined sources6
Helixi571 – 587Combined sources17
Beta strandi591 – 597Combined sources7
Helixi599 – 605Combined sources7
Helixi606 – 612Combined sources7
Beta strandi615 – 617Combined sources3
Helixi623 – 633Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6149N.
IntActiP11652. 1 interactor.
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...

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: November 2, 2016
This is version 120 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.