Skip Header

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

Probable propionyl-CoA carboxylase beta chain 6

Gene

accD6

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA.

Pathwayi: propanoyl-CoA degradation

This protein is involved in step 1 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. Probable propionyl-CoA carboxylase beta chain 5 (accD5), Probable propionyl-CoA carboxylase beta chain 6 (accD6)
  2. no protein annotated in this organism
  3. Probable methylmalonyl-CoA mutase small subunit (mutA), Probable methylmalonyl-CoA mutase large subunit (mutB)
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.

GO - Molecular functioni

  • acetyl-CoA carboxylase activity Source: MTBBASE
  • ATP binding Source: UniProtKB-KW
  • propionyl-CoA carboxylase activity Source: UniProtKB-EC

GO - Biological processi

  • fatty acid elongation, saturated fatty acid Source: MTBBASE
  • growth Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00945; UER00908.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable propionyl-CoA carboxylase beta chain 6 (EC:6.4.1.3)
Short name:
PCCase
Alternative name(s):
Propanoyl-CoA:carbon dioxide ligase
Gene namesi
Name:accD6
Ordered Locus Names:Rv2247
ORF Names:MTCY427.28
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2247.

Subcellular locationi

GO - Cellular componenti

  • acetyl-CoA carboxylase complex Source: MTBBASE
  • cell wall Source: MTBBASE
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 473472Probable propionyl-CoA carboxylase beta chain 6PRO_0000199800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP9WQH5.

Interactioni

Subunit structurei

Probably a dodecamer composed of six biotin-containing alpha subunits and six beta subunits.By similarity

Protein-protein interaction databases

STRINGi83332.Rv2247.

Structurei

Secondary structure

1
473
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 258Combined sources
Beta strandi32 – 354Combined sources
Beta strandi39 – 4911Combined sources
Beta strandi52 – 598Combined sources
Turni61 – 633Combined sources
Helixi64 – 663Combined sources
Helixi70 – 8617Combined sources
Beta strandi90 – 967Combined sources
Helixi101 – 1033Combined sources
Helixi104 – 12118Combined sources
Turni122 – 1243Combined sources
Beta strandi127 – 13610Combined sources
Helixi137 – 1404Combined sources
Helixi141 – 1455Combined sources
Beta strandi146 – 1516Combined sources
Beta strandi156 – 1605Combined sources
Helixi162 – 1698Combined sources
Helixi175 – 1795Combined sources
Helixi181 – 1866Combined sources
Beta strandi192 – 1943Combined sources
Helixi198 – 21316Combined sources
Helixi220 – 2256Combined sources
Helixi230 – 2334Combined sources
Beta strandi236 – 2405Combined sources
Helixi245 – 2517Combined sources
Beta strandi259 – 2624Combined sources
Beta strandi269 – 2768Combined sources
Beta strandi279 – 2868Combined sources
Turni288 – 2903Combined sources
Helixi291 – 2933Combined sources
Helixi297 – 31317Combined sources
Beta strandi317 – 3237Combined sources
Helixi330 – 3334Combined sources
Helixi335 – 35016Combined sources
Beta strandi355 – 36410Combined sources
Helixi365 – 3706Combined sources
Helixi374 – 3763Combined sources
Beta strandi379 – 3835Combined sources
Beta strandi388 – 3925Combined sources
Helixi394 – 3985Combined sources
Helixi403 – 4086Combined sources
Helixi411 – 42818Combined sources
Helixi432 – 4376Combined sources
Helixi447 – 4493Combined sources
Helixi450 – 46011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4L6WX-ray1.95A/B1-473[»]
ProteinModelPortaliP9WQH5.
SMRiP9WQH5. Positions 14-466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 470469CarboxyltransferaseAdd
BLAST

Sequence similaritiesi

Belongs to the AccD/PCCB family.Curated
Contains 1 carboxyltransferase domain.Curated

Phylogenomic databases

eggNOGiENOG4106H22. Bacteria.
COG4799. LUCA.
KOiK18472.
OMAiAMGVDGC.
PhylomeDBiP9WQH5.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P9WQH5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIMAPEAVG ESLDPRDPLL RLSNFFDDGS VELLHERDRS GVLAAAGTVN
60 70 80 90 100
GVRTIAFCTD GTVMGGAMGV EGCTHIVNAY DTAIEDQSPI VGIWHSGGAR
110 120 130 140 150
LAEGVRALHA VGQVFEAMIR ASGYIPQISV VVGFAAGGAA YGPALTDVVV
160 170 180 190 200
MAPESRVFVT GPDVVRSVTG EDVDMASLGG PETHHKKSGV CHIVADDELD
210 220 230 240 250
AYDRGRRLVG LFCQQGHFDR SKAEAGDTDI HALLPESSRR AYDVRPIVTA
260 270 280 290 300
ILDADTPFDE FQANWAPSMV VGLGRLSGRT VGVLANNPLR LGGCLNSESA
310 320 330 340 350
EKAARFVRLC DAFGIPLVVV VDVPGYLPGV DQEWGGVVRR GAKLLHAFGE
360 370 380 390 400
CTVPRVTLVT RKTYGGAYIA MNSRSLNATK VFAWPDAEVA VMGAKAAVGI
410 420 430 440 450
LHKKKLAAAP EHEREALHDQ LAAEHERIAG GVDSALDIGV VDEKIDPAHT
460 470
RSKLTEALAQ APARRGRHKN IPL
Length:473
Mass (Da):50,136
Last modified:April 16, 2014 - v1
Checksum:i94AD7EBD88F233C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45027.1.
PIRiC70779.
RefSeqiNP_216763.1. NC_000962.3.
WP_003900487.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP45027; CCP45027; Rv2247.
GeneIDi887671.
KEGGimtu:Rv2247.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45027.1.
PIRiC70779.
RefSeqiNP_216763.1. NC_000962.3.
WP_003900487.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4L6WX-ray1.95A/B1-473[»]
ProteinModelPortaliP9WQH5.
SMRiP9WQH5. Positions 14-466.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2247.

Proteomic databases

PaxDbiP9WQH5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP45027; CCP45027; Rv2247.
GeneIDi887671.
KEGGimtu:Rv2247.

Organism-specific databases

TubercuListiRv2247.

Phylogenomic databases

eggNOGiENOG4106H22. Bacteria.
COG4799. LUCA.
KOiK18472.
OMAiAMGVDGC.
PhylomeDBiP9WQH5.

Enzyme and pathway databases

UniPathwayiUPA00945; UER00908.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.

Entry informationi

Entry nameiPCC6_MYCTU
AccessioniPrimary (citable) accession number: P9WQH5
Secondary accession number(s): L0TBQ7, P63407, Q10506
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 11, 2015
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.