Reviewed, UniProtKB/Swiss-Prot P11653 (MUTB_PROFR)

Names and origin

Protein names

Recommended name:
    Methylmalonyl-CoA mutase large subunit
    EC=5.4.99.2
Alternative name(s):
    MCM-alpha

Gene names

Name:

mutB

Organism

Propionibacterium freudenreichii subsp. shermanii

Taxonomic identifier

1752 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Propionibacteriaceae › Propionibacterium

Protein attributes

Sequence length	728 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.
Catalytic activity	(R)-methylmalonyl-CoA = succinyl-CoA.
Cofactor	Adenosylcobalamin.
Pathway	Metabolic intermediate metabolism; propionyl-CoA degradation; succinyl-CoA from propionyl-CoA: step 3/3.
Subunit structure	Heterodimer of an alpha and a beta chain.
Sequence similarities	Belongs to the methylmalonyl-CoA mutase family. Contains 1 B12-binding domain.

Ontologies

Keywords
Ligand	Cobalamin Cobalt Metal-binding
Molecular function	Isomerase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	cobalamin binding Inferred from electronic annotation. Source: UniProtKB-KW cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW methylmalonyl-CoA mutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 728

727

Methylmalonyl-CoA mutase large subunit

PRO_0000194273

Regions

Domain

597 – 728

132

B12-binding

Region

568 – 607

40

Methylmalonyl-CoA-binding site By similarity

Sites

Metal binding

610

1

Cobalt (cobalamin axial ligand)

Secondary structure

1

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728

Helix Strand Turn

Details...

Helix

7 – 9

3

Helix

21 – 32

12

Helix

52 – 55

4

Beta strand

74 – 77

4

Helix

78 – 80

3

Helix

95 – 107

13

Beta strand

112 – 115

4

Helix

119 – 122

4

Helix

130 – 132

3

Turn

133 – 138

6

Beta strand

139 – 141

3

Helix

146 – 152

7

Turn

153 – 155

3

Turn

158 – 160

3

Beta strand

162 – 165

4

Helix

171 – 184

14

Helix

189 – 191

3

Beta strand

193 – 196

4

Helix

201 – 205

5

Helix

214 – 231

18

Beta strand

238 – 241

4

Helix

243 – 248

6

Helix

252 – 272

21

Helix

277 – 279

3

Helix

281 – 283

3

Beta strand

284 – 290

7

Helix

294 – 313

20

Helix

320 – 323

4

Beta strand

327 – 331

5

Beta strand

338 – 340

3

Helix

343 – 357

15

Beta strand

361 – 364

4

Turn

368 – 372

5

Helix

377 – 392

16

Beta strand

397 – 401

5

Turn

402 – 405

4

Helix

407 – 429

23

Helix

433 – 439

7

Helix

441 – 459

19

Beta strand

460 – 462

3

Turn

465 – 467

3

Beta strand

468 – 470

3

Helix

485 – 502

18

Helix

505 – 520

16

Helix

527 – 529

3

Helix

531 – 540

10

Helix

545 – 556

12

Helix

569 – 573

5

Turn

574 – 576

3

Helix

578 – 594

17

Beta strand

599 – 603

5

Helix

612 – 623

12

Beta strand

627 – 630

4

Helix

637 – 647

11

Beta strand

650 – 656

7

Helix

661 – 674

14

Beta strand

680 – 687

8

Helix

690 – 692

3

Helix

693 – 699

7

Beta strand

701 – 705

5

Helix

711 – 726

16

Sequences

	Sequence		Length	Mass (Da)
	P11653-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F7731C1E3C9874C0	FASTA	728	80,178
	10 20 30 40 50 60 MSTLPRFDSV DLGNAPVPAD AARRFEELAA KAGTGEAWET AEQIPVGTLF NEDVYKDMDW 70 80 90 100 110 120 LDTYAGIPPF VHGPYATMYA FRPWTIRQYA GFSTAKESNA FYRRNLAAGQ KGLSVAFDLP 130 140 150 160 170 180 THRGYDSDNP RVAGDVGMAG VAIDSIYDMR ELFAGIPLDQ MSVSMTMNGA VLPILALYVV 190 200 210 220 230 240 TAEEQGVKPE QLAGTIQNDI LKEFMVRNTY IYPPQPSMRI ISEIFAYTSA NMPKWNSISI 250 260 270 280 290 300 SGYHMQEAGA TADIEMAYTL ADGVDYIRAG ESVGLNVDQF APRLSFFWGI GMNFFMEVAK 310 320 330 340 350 360 LRAARMLWAK LVHQFGPKNP KSMSLRTHSQ TSGWSLTAQD VYNNVVRTCI EAMAATQGHT 370 380 390 400 410 420 QSLHTNSLDE AIALPTDFSA RIARNTQLFL QQESGTTRVI DPWSGSAYVE ELTWDLARKA 430 440 450 460 470 480 WGHIQEVEKV GGMAKAIEKG IPKMRIEEAA ARTQARIDSG RQPLIGVNKY RLEHEPPLDV 490 500 510 520 530 540 LKVDNSTVLA EQKAKLVKLR AERDPEKVKA ALDKITWAAG NPDDKDPDRN LLKLCIDAGR 550 560 570 580 590 600 AMATVGEMSD ALEKVFGRYT AQIRTISGVY SKEVKNTPEV EEARELVEEF EQAEGRRPRI 610 620 630 640 650 660 LLAKMGQDGH DRGQKVIATA YADLGFDVDV GPLFQTPEET ARQAVEADVH VVGVSSLAGG 670 680 690 700 710 720 HLTLVPALRK ELDKLGRPDI LITVGGVIPE QDFDELRKDG AVEIYTPGTV IPESAISLVK KLRASLDA

References

[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: 2569861] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21 AND 104-110. 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: 2569860] [Abstract] Cited for: PROTEIN SEQUENCE OF 534-537. 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: 8805541] [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: 9655823] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). Strain: NCIB 9885.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X14965 Genomic DNA. Translation: CAA33090.1.

PIR

S04641.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E1C	X-ray	2.62	A/C	2-727	[»]
1REQ	X-ray	2.00	A/C	2-728	[»]
2REQ	X-ray	2.50	A/C	2-728	[»]
3REQ	X-ray	2.70	A	2-728	[»]
4REQ	X-ray	2.20	A/C	2-728	[»]
5REQ	X-ray	2.20	A/C	2-727	[»]
6REQ	X-ray	2.20	A/C	2-727	[»]
7REQ	X-ray	2.20	A/C	2-727	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6148N.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13077.

BRENDA

5.4.99.2. 790.

Family and domain databases

InterPro

IPR006159. Acid_CoA_mut_C.
IPR014348. Cbl-dep_enz_cat-sub.
IPR006158. Cobalamin-bd.
IPR006099. MMCoA_mutase_a/b_cat.
IPR006098. MMCoA_mutase_a_cat.
[Graphical view]

Gene3D

G3DSA:3.40.50.280. B12_bd. 1 hit.
G3DSA:3.20.20.240. Cobalamin-dep_enz_cat. 1 hit.

Pfam

PF02310. B12-binding. 1 hit.
PF01642. MM_CoA_mutase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00640. acid_CoA_mut_C. 1 hit.
TIGR00641. acid_CoA_mut_N. 1 hit.

PROSITE

PS51332. B12_BINDING. 1 hit.
PS00544. METMALONYL_COA_MUTASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MUTB_PROFR

Accession

Primary (citable) accession number: P11653

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 85 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)