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Protein
Submitted name:

Propionyl-CoA carboxylase complex B subunit

Gene

pccB

Organism
Streptomyces coelicolor
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431Biotin 1
Binding sitei182 – 1821Substrate; via amide nitrogenCombined sources
Binding sitei183 – 1831Substrate; via amide nitrogenCombined sources
Binding sitei202 – 2021Biotin 1
Binding sitei202 – 2021Biotin 2
Binding sitei221 – 2211Biotin 1
Binding sitei221 – 2211Biotin 2
Sitei419 – 4191Important for catalytic activity; via amide nitrogenCombined sources
Sitei420 – 4201Important for catalytic activity; via amide nitrogenCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

BiotinCombined sources

Enzyme and pathway databases

BRENDAi6.4.1.3. 5998.

Names & Taxonomyi

Protein namesi
Submitted name:
Propionyl-CoA carboxylase complex B subunitImported
Gene namesi
Name:pccBImported
OrganismiStreptomyces coelicolorImported
Taxonomic identifieri1902 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi100226.SCO4926.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XNVX-ray2.30A/B1-530[»]
1XNWX-ray2.60A/B/C/D/E/F1-530[»]
1XNYX-ray2.20A/B1-530[»]
1XO6X-ray2.20A/B/C/D/E/F1-530[»]
3IAVX-ray1.75A/B1-530[»]
3IB9X-ray2.00A/B1-530[»]
3IBBX-ray3.50A/B/C/D/E/F1-530[»]
3MFMX-ray2.38A/B/C/D/E/F1-530[»]
ProteinModelPortaliQ9X4K7.
SMRiQ9X4K7. Positions 10-530.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X4K7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni377 – 3793Biotin 4 bindingCombined sources
Regioni417 – 4204Biotin 4 bindingCombined sources

Phylogenomic databases

HOGENOMiHOG000218693.
KOiK01966.
OrthoDBiEOG696BWK.
PhylomeDBiQ9X4K7.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000438. Acetyl_CoA_COase_Trfase_b_su.
IPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
PRINTSiPR01070. ACCCTRFRASEB.
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9X4K7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEPEEQQPD IHTTAGKLAD LRRRIEEATH AGSARAVEKQ HAKGKLTARE
60 70 80 90 100
RIDLLLDEGS FVELDEFARH RSTNFGLDAN RPYGDGVVTG YGTVDGRPVA
110 120 130 140 150
VFSQDFTVFG GALGEVYGQK IVKVMDFALK TGCPVVGIND SGGARIQEGV
160 170 180 190 200
ASLGAYGEIF RRNTHASGVI PQISLVVGPC AGGAVYSPAI TDFTVMVDQT
210 220 230 240 250
SHMFITGPDV IKTVTGEDVG FEELGGARTH NSTSGVAHHM AGDEKDAVEY
260 270 280 290 300
VKQLLSYLPS NNLSEPPAFP EEADLAVTDE DAELDTIVPD SANQPYDMHS
310 320 330 340 350
VIEHVLDDAE FFETQPLFAP NILTGFGRVE GRPVGIVANQ PMQFAGCLDI
360 370 380 390 400
TASEKAARFV RTCDAFNVPV LTFVDVPGFL PGVDQEHDGI IRRGAKLIFA
410 420 430 440 450
YAEATVPLIT VITRKAFGGA YDVMGSKHLG ADLNLAWPTA QIAVMGAQGA
460 470 480 490 500
VNILHRRTIA DAGDDAEATR ARLIQEYEDA LLNPYTAAER GYVDAVIMPS
510 520 530
DTRRHIVRGL RQLRTKRESL PPKKHGNIPL
Length:530
Mass (Da):57,159
Last modified:November 1, 1999 - v1
Checksum:i3CD6380087CFA431
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF113605 Genomic DNA. Translation: AAD28194.1.
PIRiT42208.
RefSeqiNP_629079.1. NC_003888.3.

Genome annotation databases

GeneIDi1100367.
KEGGisco:SCO4926.
PATRICi23739690. VBIStrCoe124346_5005.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF113605 Genomic DNA. Translation: AAD28194.1.
PIRiT42208.
RefSeqiNP_629079.1. NC_003888.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XNVX-ray2.30A/B1-530[»]
1XNWX-ray2.60A/B/C/D/E/F1-530[»]
1XNYX-ray2.20A/B1-530[»]
1XO6X-ray2.20A/B/C/D/E/F1-530[»]
3IAVX-ray1.75A/B1-530[»]
3IB9X-ray2.00A/B1-530[»]
3IBBX-ray3.50A/B/C/D/E/F1-530[»]
3MFMX-ray2.38A/B/C/D/E/F1-530[»]
ProteinModelPortaliQ9X4K7.
SMRiQ9X4K7. Positions 10-530.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO4926.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1100367.
KEGGisco:SCO4926.
PATRICi23739690. VBIStrCoe124346_5005.

Phylogenomic databases

HOGENOMiHOG000218693.
KOiK01966.
OrthoDBiEOG696BWK.
PhylomeDBiQ9X4K7.

Enzyme and pathway databases

BRENDAi6.4.1.3. 5998.

Miscellaneous databases

EvolutionaryTraceiQ9X4K7.

Family and domain databases

Gene3Di3.90.226.10. 2 hits.
InterProiIPR000438. Acetyl_CoA_COase_Trfase_b_su.
IPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]
PfamiPF01039. Carboxyl_trans. 1 hit.
[Graphical view]
PRINTSiPR01070. ACCCTRFRASEB.
SUPFAMiSSF52096. SSF52096. 2 hits.
PROSITEiPS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Gramajo H.C., Rodriguez E.J., Danchin A.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A3Imported.
  2. "Genetic and biochemical characterization of the alpha and beta components of a propionyl-CoA carboxylase complex of Streptomyces coelicolor A3(2)."
    Rodriguez E., Gramajo H.
    Microbiology 145:3109-3119(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: A3Imported.
  3. "Crystal structure of the beta-subunit of acyl-CoA carboxylase: structure-based engineering of substrate specificity."
    Diacovich L., Mitchell D.L., Pham H., Gago G., Melgar M.M., Khosla C., Gramajo H., Tsai S.C.
    Biochemistry 43:14027-14036(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH BIOTIN.
  4. "Crystal structures and mutational analyses of acyl-CoA carboxylase beta subunit of Streptomyces coelicolor."
    Arabolaza A., Shillito M.E., Lin T.W., Diacovich L., Melgar M., Pham H., Amick D., Gramajo H., Tsai S.C.
    Biochemistry 49:7367-7376(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH BIOTIN.

Entry informationi

Entry nameiQ9X4K7_STRCH
AccessioniPrimary (citable) accession number: Q9X4K7
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1999
Last sequence update: November 1, 1999
Last modified: June 24, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.