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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)DescriptionActionsGraphical viewLength
Metal bindingi610Cobalt (cobalamin axial ligand)1

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001942732 – 728Methylmalonyl-CoA mutase large subunitAdd BLAST727

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 interactor.
MINTiMINT-1536014.
STRINGi754252.PFREUD_07650.

Structurei

Secondary structure

1728
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 9Combined sources3
Helixi21 – 32Combined sources12
Helixi52 – 55Combined sources4
Turni59 – 62Combined sources4
Beta strandi74 – 77Combined sources4
Helixi78 – 80Combined sources3
Beta strandi85 – 90Combined sources6
Helixi95 – 107Combined sources13
Beta strandi112 – 115Combined sources4
Helixi119 – 123Combined sources5
Beta strandi127 – 129Combined sources3
Helixi130 – 135Combined sources6
Turni136 – 138Combined sources3
Beta strandi139 – 141Combined sources3
Helixi146 – 152Combined sources7
Turni153 – 155Combined sources3
Turni158 – 160Combined sources3
Beta strandi162 – 165Combined sources4
Beta strandi168 – 170Combined sources3
Helixi171 – 184Combined sources14
Helixi189 – 191Combined sources3
Beta strandi193 – 196Combined sources4
Helixi201 – 205Combined sources5
Helixi214 – 231Combined sources18
Beta strandi238 – 241Combined sources4
Helixi243 – 248Combined sources6
Helixi252 – 272Combined sources21
Helixi277 – 279Combined sources3
Helixi281 – 283Combined sources3
Beta strandi284 – 290Combined sources7
Helixi294 – 313Combined sources20
Helixi320 – 323Combined sources4
Beta strandi327 – 331Combined sources5
Helixi333 – 335Combined sources3
Beta strandi338 – 340Combined sources3
Helixi343 – 357Combined sources15
Beta strandi361 – 364Combined sources4
Turni368 – 372Combined sources5
Helixi377 – 392Combined sources16
Beta strandi398 – 401Combined sources4
Turni402 – 405Combined sources4
Helixi407 – 429Combined sources23
Helixi433 – 439Combined sources7
Helixi441 – 458Combined sources18
Beta strandi460 – 462Combined sources3
Turni465 – 467Combined sources3
Beta strandi468 – 470Combined sources3
Helixi485 – 502Combined sources18
Helixi505 – 520Combined sources16
Helixi527 – 529Combined sources3
Helixi531 – 540Combined sources10
Helixi545 – 556Combined sources12
Helixi570 – 573Combined sources4
Turni574 – 576Combined sources3
Helixi578 – 594Combined sources17
Beta strandi599 – 603Combined sources5
Beta strandi605 – 607Combined sources3
Helixi612 – 623Combined sources12
Beta strandi627 – 630Combined sources4
Beta strandi633 – 635Combined sources3
Helixi637 – 646Combined sources10
Beta strandi650 – 656Combined sources7
Helixi661 – 674Combined sources14
Beta strandi680 – 687Combined sources8
Helixi690 – 692Combined sources3
Helixi693 – 698Combined sources6
Beta strandi701 – 705Combined sources5
Helixi711 – 726Combined sources16

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP11653.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini597 – 728B12-bindingPROSITE-ProRule annotationAdd BLAST132

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni568 – 607Methylmalonyl-CoA-binding siteBy similarityAdd BLAST40

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6148N.
IntActiP11653. 1 interactor.
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: November 2, 2016
This is version 123 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.