P27253 (SCPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methylmalonyl-CoA mutase
Short name=MCM
EC=5.4.99.2

Gene names

Name:	scpA
Synonyms:	sbm, yliK
Ordered Locus Names:	b2917, JW2884

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	714 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the interconversion of succinyl-CoA and methylmalonyl-CoA. Could be part of a pathway that converts succinate to propionate. Ref.4 Ref.5
Catalytic activity	(R)-methylmalonyl-CoA = succinyl-CoA. Ref.4 Ref.5
Cofactor	Adenosylcobalamin. Ref.4 Ref.5
Subunit structure	Homodimer. Interacts with ArgK. Ref.6
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	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	cobalamin binding Inferred from direct assay Ref.4. Source: EcoCyc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW methylmalonyl-CoA mutase activity Inferred from direct assay Ref.4. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 714	714	Methylmalonyl-CoA mutase		PRO_0000194277
Regions
	Domain	584 – 714	131	B12-binding
Sites
	Metal binding	597	1	Cobalt (cobalamin axial ligand) By similarity
Experimental info
	Sequence conflict	356	1	A → V in CAA47311. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P27253 [UniParc]. Last modified August 29, 2003. Version 2. Checksum: 65222F5EB2F4633A	FASTA	714	77,871
	10 20 30 40 50 60 MSNVQEWQQL ANKELSRREK TVDSLVHQTA EGIAIKPLYT EADLDNLEVT GTLPGLPPYV 70 80 90 100 110 120 RGPRATMYTA QPWTIRQYAG FSTAKESNAF YRRNLAAGQK GLSVAFDLAT HRGYDSDNPR 130 140 150 160 170 180 VAGDVGKAGV AIDTVEDMKV LFDQIPLDKM SVSMTMNGAV LPVLAFYIVA AEEQGVTPDK 190 200 210 220 230 240 LTGTIQNDIL KEYLCRNTYI YPPKPSMRII ADIIAWCSGN MPRFNTISIS GYHMGEAGAN 250 260 270 280 290 300 CVQQVAFTLA DGIEYIKAAI SAGLKIDDFA PRLSFFFGIG MDLFMNVAML RAARYLWSEA 310 320 330 340 350 360 VSGFGAQDPK SLALRTHCQT SGWSLTEQDP YNNVIRTTIE ALAATLGGTQ SLHTNAFDEA 370 380 390 400 410 420 LGLPTDFSAR IARNTQIIIQ EESELCRTVD PLAGSYYIES LTDQIVKQAR AIIQQIDEAG 430 440 450 460 470 480 GMAKAIEAGL PKRMIEEASA REQSLIDQGK RVIVGVNKYK LDHEDETDVL EIDNVMVRNE 490 500 510 520 530 540 QIASLERIRA TRDDAAVTAA LNALTHAAQH NENLLAAAVN AARVRATLGE ISDALEVAFD 550 560 570 580 590 600 RYLVPSQCVT GVIAQSYHQS EKSASEFDAI VAQTEQFLAD NGRRPRILIA KMGQDGHDRG 610 620 630 640 650 660 AKVIASAYSD LGFDVDLSPM FSTPEEIARL AVENDVHVVG ASSLAAGHKT LIPELVEALK 670 680 690 700 710 KWGREDICVV AGGVIPPQDY AFLQERGVAA IYGPGTPMLD SVRDVLNLIS QHHD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Physical map location of the new Escherichia coli gene sbm." Roy I., Leadlay P.F. J. Bacteriol. 174:5763-5764(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Discovering new enzymes and metabolic pathways: conversion of succinate to propionate by Escherichia coli." Haller T., Buckel T., Retey J., Gerlt J.A. Biochemistry 39:4622-4629(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Metabolic engineering of a methylmalonyl-CoA mutase-epimerase pathway for complex polyketide biosynthesis in Escherichia coli." Dayem L.C., Carney J.R., Santi D.V., Pfeifer B.A., Khosla C., Kealey J.T. Biochemistry 41:5193-5201(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
[6]	"Sleeping beauty mutase (sbm) is expressed and interacts with ygfd in Escherichia coli." Froese D.S., Dobson C.M., White A.P., Wu X., Padovani D., Banerjee R., Haller T., Gerlt J.A., Surette M.G., Gravel R.A. Microbiol. Res. 164:1-8(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, INTERACTION WITH ARGK.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X66836 Genomic DNA. Translation: CAA47311.1. U28377 Genomic DNA. Translation: AAA69084.1. U00096 Genomic DNA. Translation: AAC75954.1. AP009048 Genomic DNA. Translation: BAE76981.1.
PIR	D65076.
RefSeq	NP_417392.1. NC_000913.2. YP_491117.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P27253.
SMR	P27253. Positions 28-701.
ModBase	Search...
Protein-protein interaction databases
IntAct	P27253. 6 interactions.
STRING	511145.b2917.
Proteomic databases
PaxDb	P27253.
PRIDE	P27253.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75954; AAC75954; b2917. BAE76981; BAE76981; BAE76981.
GeneID	12933336. 945576.
KEGG	ecj:Y75_p2848. eco:b2917.
PATRIC	32121248. VBIEscCol129921_3012.
Organism-specific databases
EchoBASE	EB1414.
EcoGene	EG11444. scpA.
Phylogenomic databases
eggNOG	COG2185.
HOGENOM	HOG000003917.
KO	K01847.
OMA	AGHKTLA.
ProtClustDB	PRK09426.
Enzyme and pathway databases
BioCyc	EcoCyc:METHYLMALONYL-COA-MUT-MONOMER. ECOL316407:JW2884-MONOMER. MetaCyc:METHYLMALONYL-COA-MUT-MONOMER.
Gene expression databases
Genevestigator	P27253.
Family and domain databases
Gene3D	3.20.20.240. 1 hit. 3.40.50.280. 1 hit.
InterPro	IPR006159. 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]
Pfam	PF02310. B12-binding. 1 hit. PF01642. MM_CoA_mutase. 1 hit. [Graphical view]
SUPFAM	SSF52242. Cbl-bd. 1 hit. SSF51703. Cbl-dep_enz_cat. 1 hit.
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

SCPA_ECOLI

Accession

Primary (citable) accession number: P27253
Secondary accession number(s): Q2M9S5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 29, 2003
Last modified:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program