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Q9X4K7

- Q9X4K7_STRCH

UniProt

Q9X4K7 - Q9X4K7_STRCH

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Protein
Submitted name: Propionyl-CoA carboxylase complex B subunit
Gene
pccB
Organism
Streptomyces coelicolor
Status
Unreviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431Biotin 1Imported
Binding sitei74 – 741Sulfate 3
Binding sitei182 – 1821Substrate; via amide nitrogenImported
Binding sitei183 – 1831Substrate; via amide nitrogenImported
Binding sitei202 – 2021Biotin 1Imported
Binding sitei202 – 2021Biotin 2Imported
Binding sitei221 – 2211Biotin 1Imported
Binding sitei221 – 2211Biotin 2Imported
Sitei419 – 4191Important for catalytic activity; via amide nitrogenImported
Sitei420 – 4201Important for catalytic activity; via amide nitrogenImported
Binding sitei490 – 4901Sulfate 3

GO - Molecular functioni

  1. acetyl-CoA carboxylase activity Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Ligandi

BiotinImported

Names & Taxonomyi

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

Subcellular locationi

GO - Cellular componenti

  1. acetyl-CoA carboxylase complex Source: InterPro
Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi100226.SCO4926.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ9X4K7.

Family & Domainsi

Region

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

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

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MSEPEEQQPD IHTTAGKLAD LRRRIEEATH AGSARAVEKQ HAKGKLTARE    50
RIDLLLDEGS FVELDEFARH RSTNFGLDAN RPYGDGVVTG YGTVDGRPVA 100
VFSQDFTVFG GALGEVYGQK IVKVMDFALK TGCPVVGIND SGGARIQEGV 150
ASLGAYGEIF RRNTHASGVI PQISLVVGPC AGGAVYSPAI TDFTVMVDQT 200
SHMFITGPDV IKTVTGEDVG FEELGGARTH NSTSGVAHHM AGDEKDAVEY 250
VKQLLSYLPS NNLSEPPAFP EEADLAVTDE DAELDTIVPD SANQPYDMHS 300
VIEHVLDDAE FFETQPLFAP NILTGFGRVE GRPVGIVANQ PMQFAGCLDI 350
TASEKAARFV RTCDAFNVPV LTFVDVPGFL PGVDQEHDGI IRRGAKLIFA 400
YAEATVPLIT VITRKAFGGA YDVMGSKHLG ADLNLAWPTA QIAVMGAQGA 450
VNILHRRTIA DAGDDAEATR ARLIQEYEDA LLNPYTAAER GYVDAVIMPS 500
DTRRHIVRGL RQLRTKRESL PPKKHGNIPL 530
Length:530
Mass (Da):57,159
Last modified:November 1, 1999 - v1
Checksum:i3CD6380087CFA431
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF113605 Genomic DNA. Translation: AAD28194.1 .
PIRi T42208.
RefSeqi NP_629079.1. NC_003888.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XNV X-ray 2.30 A/B 1-530 [» ]
1XNW X-ray 2.60 A/B/C/D/E/F 1-530 [» ]
1XNY X-ray 2.20 A/B 1-530 [» ]
1XO6 X-ray 2.20 A/B/C/D/E/F 1-530 [» ]
3IAV X-ray 1.75 A/B 1-530 [» ]
3IB9 X-ray 2.00 A/B 1-530 [» ]
3IBB X-ray 3.50 A/B/C/D/E/F 1-530 [» ]
3MFM X-ray 2.38 A/B/C/D/E/F 1-530 [» ]
ProteinModelPortali Q9X4K7.
SMRi Q9X4K7. Positions 10-530.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 100226.SCO4926.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1100367.
KEGGi sco:SCO4926.
PATRICi 23739690. VBIStrCoe124346_5005.

Phylogenomic databases

HOGENOMi HOG000218693.
KOi K01966.
OrthoDBi EOG696BWK.
PhylomeDBi Q9X4K7.

Miscellaneous databases

EvolutionaryTracei Q9X4K7.

Family and domain databases

Gene3Di 3.90.226.10. 2 hits.
InterProi IPR000438. Acetyl_CoA_COase_Trfase_b_su.
IPR000022. Carboxyl_trans.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view ]
Pfami PF01039. Carboxyl_trans. 1 hit.
[Graphical view ]
PRINTSi PR01070. ACCCTRFRASEB.
SUPFAMi SSF52096. SSF52096. 2 hits.
PROSITEi PS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 AND GLYCINE RADICAL, ACTIVE SITE.
  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: September 3, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

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