Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P27253

- SCPA_ECOLI

UniProt

P27253 - SCPA_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Methylmalonyl-CoA mutase

Gene

scpA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the interconversion of succinyl-CoA and methylmalonyl-CoA. Could be part of a pathway that converts succinate to propionate.2 Publications

Catalytic activityi

(R)-methylmalonyl-CoA = succinyl-CoA.2 Publications

Cofactori

adenosylcob(III)alamin2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi597 – 5971Cobalt (cobalamin axial ligand)By similarity

GO - Molecular functioni

  1. cobalamin binding Source: EcoCyc
  2. metal ion binding Source: UniProtKB-KW
  3. methylmalonyl-CoA mutase activity Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Cobalamin, Cobalt, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:METHYLMALONYL-COA-MUT-MONOMER.
ECOL316407:JW2884-MONOMER.
MetaCyc:METHYLMALONYL-COA-MUT-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylmalonyl-CoA mutase (EC:5.4.99.2)
Short name:
MCM
Gene namesi
Name:scpA
Synonyms:sbm, yliK
Ordered Locus Names:b2917, JW2884
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11444. scpA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 714714Methylmalonyl-CoA mutasePRO_0000194277Add
BLAST

Proteomic databases

PaxDbiP27253.
PRIDEiP27253.

Expressioni

Gene expression databases

GenevestigatoriP27253.

Interactioni

Subunit structurei

Homodimer. Interacts with ArgK.1 Publication

Protein-protein interaction databases

IntActiP27253. 6 interactions.
STRINGi511145.b2917.

Structurei

3D structure databases

ProteinModelPortaliP27253.
SMRiP27253. Positions 28-701.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini584 – 714131B12-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG2185.
HOGENOMiHOG000003917.
InParanoidiP27253.
KOiK01847.
OMAiSIYDMRQ.
OrthoDBiEOG6423BW.
PhylomeDBiP27253.

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.

P27253-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNVQEWQQL ANKELSRREK TVDSLVHQTA EGIAIKPLYT EADLDNLEVT
60 70 80 90 100
GTLPGLPPYV RGPRATMYTA QPWTIRQYAG FSTAKESNAF YRRNLAAGQK
110 120 130 140 150
GLSVAFDLAT HRGYDSDNPR VAGDVGKAGV AIDTVEDMKV LFDQIPLDKM
160 170 180 190 200
SVSMTMNGAV LPVLAFYIVA AEEQGVTPDK LTGTIQNDIL KEYLCRNTYI
210 220 230 240 250
YPPKPSMRII ADIIAWCSGN MPRFNTISIS GYHMGEAGAN CVQQVAFTLA
260 270 280 290 300
DGIEYIKAAI SAGLKIDDFA PRLSFFFGIG MDLFMNVAML RAARYLWSEA
310 320 330 340 350
VSGFGAQDPK SLALRTHCQT SGWSLTEQDP YNNVIRTTIE ALAATLGGTQ
360 370 380 390 400
SLHTNAFDEA LGLPTDFSAR IARNTQIIIQ EESELCRTVD PLAGSYYIES
410 420 430 440 450
LTDQIVKQAR AIIQQIDEAG GMAKAIEAGL PKRMIEEASA REQSLIDQGK
460 470 480 490 500
RVIVGVNKYK LDHEDETDVL EIDNVMVRNE QIASLERIRA TRDDAAVTAA
510 520 530 540 550
LNALTHAAQH NENLLAAAVN AARVRATLGE ISDALEVAFD RYLVPSQCVT
560 570 580 590 600
GVIAQSYHQS EKSASEFDAI VAQTEQFLAD NGRRPRILIA KMGQDGHDRG
610 620 630 640 650
AKVIASAYSD LGFDVDLSPM FSTPEEIARL AVENDVHVVG ASSLAAGHKT
660 670 680 690 700
LIPELVEALK KWGREDICVV AGGVIPPQDY AFLQERGVAA IYGPGTPMLD
710
SVRDVLNLIS QHHD
Length:714
Mass (Da):77,871
Last modified:August 29, 2003 - v2
Checksum:i65222F5EB2F4633A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti356 – 3561A → V in CAA47311. (PubMed:1355087)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66836 Genomic DNA. Translation: CAA47311.1.
U28377 Genomic DNA. Translation: AAA69084.1.
U00096 Genomic DNA. Translation: AAC75954.1.
AP009048 Genomic DNA. Translation: BAE76981.1.
PIRiD65076.
RefSeqiNP_417392.1. NC_000913.3.
YP_491117.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75954; AAC75954; b2917.
BAE76981; BAE76981; BAE76981.
GeneIDi12933336.
945576.
KEGGiecj:Y75_p2848.
eco:b2917.
PATRICi32121248. VBIEscCol129921_3012.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66836 Genomic DNA. Translation: CAA47311.1 .
U28377 Genomic DNA. Translation: AAA69084.1 .
U00096 Genomic DNA. Translation: AAC75954.1 .
AP009048 Genomic DNA. Translation: BAE76981.1 .
PIRi D65076.
RefSeqi NP_417392.1. NC_000913.3.
YP_491117.1. NC_007779.1.

3D structure databases

ProteinModelPortali P27253.
SMRi P27253. Positions 28-701.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P27253. 6 interactions.
STRINGi 511145.b2917.

Proteomic databases

PaxDbi P27253.
PRIDEi P27253.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75954 ; AAC75954 ; b2917 .
BAE76981 ; BAE76981 ; BAE76981 .
GeneIDi 12933336.
945576.
KEGGi ecj:Y75_p2848.
eco:b2917.
PATRICi 32121248. VBIEscCol129921_3012.

Organism-specific databases

EchoBASEi EB1414.
EcoGenei EG11444. scpA.

Phylogenomic databases

eggNOGi COG2185.
HOGENOMi HOG000003917.
InParanoidi P27253.
KOi K01847.
OMAi SIYDMRQ.
OrthoDBi EOG6423BW.
PhylomeDBi P27253.

Enzyme and pathway databases

BioCyci EcoCyc:METHYLMALONYL-COA-MUT-MONOMER.
ECOL316407:JW2884-MONOMER.
MetaCyc:METHYLMALONYL-COA-MUT-MONOMER.

Miscellaneous databases

PROi P27253.

Gene expression databases

Genevestigatori P27253.

Family and domain databases

Gene3Di 3.20.20.240. 1 hit.
3.40.50.280. 1 hit.
InterProi 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 ]
Pfami PF02310. B12-binding. 1 hit.
PF01642. MM_CoA_mutase. 1 hit.
[Graphical view ]
SUPFAMi SSF51703. SSF51703. 1 hit.
SSF52242. SSF52242. 1 hit.
TIGRFAMsi TIGR00640. acid_CoA_mut_C. 1 hit.
TIGR00641. acid_CoA_mut_N. 1 hit.
PROSITEi PS51332. B12_BINDING. 1 hit.
PS00544. METMALONYL_COA_MUTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiSCPA_ECOLI
AccessioniPrimary (citable) accession number: P27253
Secondary accession number(s): Q2M9S5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 29, 2003
Last modified: November 26, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3