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Protein

Methylmalonyl-CoA mutase large subunit

Gene

mutB

Organism
Propionibacterium freudenreichii subsp. shermanii
Status
Reviewed-Annotation score: Annotation score: 5 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi610 – 6101Cobalt (cobalamin axial ligand)

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalamin, Cobalt, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13077.
BRENDAi5.4.99.2. 5032.
SABIO-RKP11653.
UniPathwayiUPA00945; UER00910.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylmalonyl-CoA mutase large subunit (EC:5.4.99.2)
Alternative name(s):
MCM-alpha
Gene namesi
Name:mutB
OrganismiPropionibacterium freudenreichii subsp. shermanii
Taxonomic identifieri1752 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPropionibacterialesPropionibacteriaceaePropionibacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 728727Methylmalonyl-CoA mutase large subunitPRO_0000194273Add
BLAST

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Binary interactionsi

WithEntry#Exp.IntActNotes
mutAP116524EBI-1027336,EBI-1027328

Protein-protein interaction databases

DIPiDIP-6148N.
IntActiP11653. 1 interaction.
MINTiMINT-1536014.
STRINGi754252.PFREUD_07650.

Structurei

Secondary structure

1
728
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 93Combined sources
Helixi21 – 3212Combined sources
Helixi52 – 554Combined sources
Turni59 – 624Combined sources
Beta strandi74 – 774Combined sources
Helixi78 – 803Combined sources
Beta strandi85 – 906Combined sources
Helixi95 – 10713Combined sources
Beta strandi112 – 1154Combined sources
Helixi119 – 1235Combined sources
Beta strandi127 – 1293Combined sources
Helixi130 – 1356Combined sources
Turni136 – 1383Combined sources
Beta strandi139 – 1413Combined sources
Helixi146 – 1527Combined sources
Turni153 – 1553Combined sources
Turni158 – 1603Combined sources
Beta strandi162 – 1654Combined sources
Beta strandi168 – 1703Combined sources
Helixi171 – 18414Combined sources
Helixi189 – 1913Combined sources
Beta strandi193 – 1964Combined sources
Helixi201 – 2055Combined sources
Helixi214 – 23118Combined sources
Beta strandi238 – 2414Combined sources
Helixi243 – 2486Combined sources
Helixi252 – 27221Combined sources
Helixi277 – 2793Combined sources
Helixi281 – 2833Combined sources
Beta strandi284 – 2907Combined sources
Helixi294 – 31320Combined sources
Helixi320 – 3234Combined sources
Beta strandi327 – 3315Combined sources
Helixi333 – 3353Combined sources
Beta strandi338 – 3403Combined sources
Helixi343 – 35715Combined sources
Beta strandi361 – 3644Combined sources
Turni368 – 3725Combined sources
Helixi377 – 39216Combined sources
Beta strandi398 – 4014Combined sources
Turni402 – 4054Combined sources
Helixi407 – 42923Combined sources
Helixi433 – 4397Combined sources
Helixi441 – 45818Combined sources
Beta strandi460 – 4623Combined sources
Turni465 – 4673Combined sources
Beta strandi468 – 4703Combined sources
Helixi485 – 50218Combined sources
Helixi505 – 52016Combined sources
Helixi527 – 5293Combined sources
Helixi531 – 54010Combined sources
Helixi545 – 55612Combined sources
Helixi570 – 5734Combined sources
Turni574 – 5763Combined sources
Helixi578 – 59417Combined sources
Beta strandi599 – 6035Combined sources
Beta strandi605 – 6073Combined sources
Helixi612 – 62312Combined sources
Beta strandi627 – 6304Combined sources
Beta strandi633 – 6353Combined sources
Helixi637 – 64610Combined sources
Beta strandi650 – 6567Combined sources
Helixi661 – 67414Combined sources
Beta strandi680 – 6878Combined sources
Helixi690 – 6923Combined sources
Helixi693 – 6986Combined sources
Beta strandi701 – 7055Combined sources
Helixi711 – 72616Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E1CX-ray2.62A/C2-728[»]
1REQX-ray2.00A/C2-728[»]
2REQX-ray2.50A/C2-728[»]
3REQX-ray2.70A2-728[»]
4REQX-ray2.20A/C2-728[»]
5REQX-ray2.20A/C2-728[»]
6REQX-ray2.20A/C2-728[»]
7REQX-ray2.20A/C2-728[»]
ProteinModelPortaliP11653.
SMRiP11653. Positions 2-728.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11653.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini597 – 728132B12-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni568 – 60740Methylmalonyl-CoA-binding siteBy similarityAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105D5P. Bacteria.
COG1884. LUCA.
COG2185. LUCA.

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.

P11653-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTLPRFDSV DLGNAPVPAD AARRFEELAA KAGTGEAWET AEQIPVGTLF
60 70 80 90 100
NEDVYKDMDW LDTYAGIPPF VHGPYATMYA FRPWTIRQYA GFSTAKESNA
110 120 130 140 150
FYRRNLAAGQ KGLSVAFDLP THRGYDSDNP RVAGDVGMAG VAIDSIYDMR
160 170 180 190 200
ELFAGIPLDQ MSVSMTMNGA VLPILALYVV TAEEQGVKPE QLAGTIQNDI
210 220 230 240 250
LKEFMVRNTY IYPPQPSMRI ISEIFAYTSA NMPKWNSISI SGYHMQEAGA
260 270 280 290 300
TADIEMAYTL ADGVDYIRAG ESVGLNVDQF APRLSFFWGI GMNFFMEVAK
310 320 330 340 350
LRAARMLWAK LVHQFGPKNP KSMSLRTHSQ TSGWSLTAQD VYNNVVRTCI
360 370 380 390 400
EAMAATQGHT QSLHTNSLDE AIALPTDFSA RIARNTQLFL QQESGTTRVI
410 420 430 440 450
DPWSGSAYVE ELTWDLARKA WGHIQEVEKV GGMAKAIEKG IPKMRIEEAA
460 470 480 490 500
ARTQARIDSG RQPLIGVNKY RLEHEPPLDV LKVDNSTVLA EQKAKLVKLR
510 520 530 540 550
AERDPEKVKA ALDKITWAAG NPDDKDPDRN LLKLCIDAGR AMATVGEMSD
560 570 580 590 600
ALEKVFGRYT AQIRTISGVY SKEVKNTPEV EEARELVEEF EQAEGRRPRI
610 620 630 640 650
LLAKMGQDGH DRGQKVIATA YADLGFDVDV GPLFQTPEET ARQAVEADVH
660 670 680 690 700
VVGVSSLAGG HLTLVPALRK ELDKLGRPDI LITVGGVIPE QDFDELRKDG
710 720
AVEIYTPGTV IPESAISLVK KLRASLDA
Length:728
Mass (Da):80,178
Last modified:January 23, 2007 - v3
Checksum:iF7731C1E3C9874C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14965 Genomic DNA. Translation: CAA33090.1.
PIRiS04641.
RefSeqiWP_044636063.1. NZ_LN997841.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14965 Genomic DNA. Translation: CAA33090.1.
PIRiS04641.
RefSeqiWP_044636063.1. NZ_LN997841.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E1CX-ray2.62A/C2-728[»]
1REQX-ray2.00A/C2-728[»]
2REQX-ray2.50A/C2-728[»]
3REQX-ray2.70A2-728[»]
4REQX-ray2.20A/C2-728[»]
5REQX-ray2.20A/C2-728[»]
6REQX-ray2.20A/C2-728[»]
7REQX-ray2.20A/C2-728[»]
ProteinModelPortaliP11653.
SMRiP11653. Positions 2-728.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6148N.
IntActiP11653. 1 interaction.
MINTiMINT-1536014.
STRINGi754252.PFREUD_07650.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105D5P. Bacteria.
COG1884. LUCA.
COG2185. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00945; UER00910.
BioCyciMetaCyc:MONOMER-13077.
BRENDAi5.4.99.2. 5032.
SABIO-RKP11653.

Miscellaneous databases

EvolutionaryTraceiP11653.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiMUTB_PROFR
AccessioniPrimary (citable) accession number: P11653
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 121 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.