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B1MNR6 (B1MNR6_MYCA9) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component PIRNR PIRNR000156
EC=1.2.4.1 PIRNR PIRNR000156
Gene names
Ordered Locus Names:MAB_1884c
OrganismMycobacterium abscessus (strain ATCC 19977 / DSM 44196) [Complete proteome] [HAMAP]
Taxonomic identifier561007 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium abscessus

Protein attributes

Sequence length905 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. PIRNR PIRNR000156

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. PIRNR PIRNR000156

Cofactor

Thiamine pyrophosphate By similarity. PIRNR PIRNR000156

Sequences

Sequence LengthMass (Da)Tools
B1MNR6 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 441F55901967B10A

FASTA905100,435
        10         20         30         40         50         60 
MIREGVASYL PDIDPDETGE WLESFDGLLA RSGPARARYL MLRLLERANA GRVAIPALTS 

        70         80         90        100        110        120 
TDYVNTIPTE NEPWFPGDED TERRFRAWIR WNAAIMVHRA QRPGVGVGGH ISTYASSAAL 

       130        140        150        160        170        180 
YEVGFNHFFR GNAHPGGGDQ IFIQGHASPG IYARAFLEGR LTTDQLDGFR QEKSHPGGGL 

       190        200        210        220        230        240 
PSYPHPRLMP DFWQFPTVSM GLGPMNAIMQ ARFNHYLRDR GIKDTSDQRV WAFLGDGEMD 

       250        260        270        280        290        300 
EPESRGLAHI AATEGLDNLT FVVNCNLQRL DGPVRGNGKI IQELESFFRG AGWNVIKVVW 

       310        320        330        340        350        360 
GREWDALLHA DRDGALVNLM NTTADGDYQT YKANDGAYVR EHFFGRDPRT KELVKDLTDA 

       370        380        390        400        410        420 
QVWNLKRGGH DYRKVYAAYR AATEHKGQPT VILAKTIKGY TLGKHFEGRN ATHQMKKLTL 

       430        440        450        460        470        480 
DDLKDFRDKQ RIPISDAQLE ENPYLPPYYH PGPEAPEIRY MLDRRRALGG FVPSRRTTSR 

       490        500        510        520        530        540 
PLTLPGSETY ASIKKGSGKQ EVATTMALVR TFKELLRDKN IGNRIVPIIP DEARTFGMDS 

       550        560        570        580        590        600 
WFPSLKIYNR NGQLYTSVDA ELMLAYKESA QGQILHEGIN EAGSTASFTA VGTAYSTHDE 

       610        620        630        640        650        660 
PMIPLYIFYS MFGFQRTGDG LWAAADQMAR GFVLGATAGR TTLTGEGLQH ADGHSLLLAS 

       670        680        690        700        710        720 
TNPAVVAYDP AFAYEIAHIV EHGLQRMYGE NSENVYFYIT LYNEPYVQPA EPENVDTEGI 

       730        740        750        760        770        780 
LRGIYKFRAA PEARTHRANI LASGVSVPDA LRAADLLAEQ WDVAADVWSV TSWGELNRDG 

       790        800        810        820        830        840 
LAIDHQALRH PDRPKGVPYV TKALEGAQGP KVAVSDWMHA VPEQIRPWVP GMYRTLGADG 

       850        860        870        880        890        900 
FGISDTRPAA RRFFNTDAES VVVAVLEALA DEGSVDRQVA VTAAAQYKID DVSAADVSYK 


DTGSA

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References

[1]"Acquisition of foreign virulence genes by the cystic fibrosis pathogen Mycobacterium abscessus."
Genoscope
Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., Gaillard J.L.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU458896 Genomic DNA. Translation: CAM61967.1.
RefSeqYP_001702621.1. NC_010397.1.

3D structure databases

ProteinModelPortalB1MNR6.
SMRB1MNR6. Positions 61-892.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1MNR6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000004771; EBMYCP00000004710; EBMYCG00000004769.
GeneID5964399.
GenomeReviewsGene locus MAB_1884c in contig CU458896_GR.
KEGGmab:MAB_1884c.
PATRIC17975471. VBIMycAbs55940_1918.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000016271.
HOGENOMHBG289271.
OMAFRQEKSH.
ProtClustDBPRK09405.

Family and domain databases

InterProIPR004660. 2-oxoA_DH_E1.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005474. Transketolase_N.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
KOK00163.
PANTHERPTHR11624:SF37. PTHR11624:SF37. 1 hit.
PfamPF00456. Transketolase_N. 2 hits.
[Graphical view]
PIRSFPIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00759. AceE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB1MNR6_MYCA9
AccessionPrimary (citable) accession number: B1MNR6
Entry history
Integrated into UniProtKB/TrEMBL: April 29, 2008
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info