Propionyl-CoA carboxylase complex B subunit

Preferred order of sections

Names and origin

Protein names

Submitted name:
Propionyl-CoA carboxylase complex B subunit EMBL AAD28194.1

Gene names

Name:

pccB EMBL AAD28194.1

Organism

Streptomyces coelicolor EMBL AAD28194.1

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Biotin PDB 1XNY PDB 3IB9
Technical term	3D-structure PDB 1XNV PDB 1XNW PDB 1XNY PDB 1XO6 PDB 3IAV PDB 3IB9 PDB 3IBB PDB 3MFM
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	acetyl-CoA carboxylase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Region

377 – 379

3

Biotin 4 binding PDB 1XNY

Region

417 – 420

4

Biotin 4 binding PDB 1XNY

Sites

Binding site

43

1

Biotin 1 PDB 3IB9

Binding site

182

1

Substrate; via amide nitrogen PDB 1XNY

Binding site

183

1

Substrate; via amide nitrogen PDB 1XNY

Binding site

202

1

Biotin 1 PDB 3IB9

Binding site

202

1

Biotin 2 PDB 3IB9

Binding site

221

1

Biotin 1 PDB 3IB9

Binding site

221

1

Biotin 2 PDB 3IB9

Site

419

1

Important for catalytic activity; via amide nitrogen PDB 1XNY

Site

420

1

Important for catalytic activity; via amide nitrogen PDB 1XNY

Sequences

Sequence

Length

Mass (Da)

Tools

Q9X4K7 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 3CD6380087CFA431
Show »

FASTA

530

57,159

        10         20         30         40         50         60 
MSEPEEQQPD IHTTAGKLAD LRRRIEEATH AGSARAVEKQ HAKGKLTARE RIDLLLDEGS 

        70         80         90        100        110        120 
FVELDEFARH RSTNFGLDAN RPYGDGVVTG YGTVDGRPVA VFSQDFTVFG GALGEVYGQK 

       130        140        150        160        170        180 
IVKVMDFALK TGCPVVGIND SGGARIQEGV ASLGAYGEIF RRNTHASGVI PQISLVVGPC 

       190        200        210        220        230        240 
AGGAVYSPAI TDFTVMVDQT SHMFITGPDV IKTVTGEDVG FEELGGARTH NSTSGVAHHM 

       250        260        270        280        290        300 
AGDEKDAVEY VKQLLSYLPS NNLSEPPAFP EEADLAVTDE DAELDTIVPD SANQPYDMHS 

       310        320        330        340        350        360 
VIEHVLDDAE FFETQPLFAP NILTGFGRVE GRPVGIVANQ PMQFAGCLDI TASEKAARFV 

       370        380        390        400        410        420 
RTCDAFNVPV LTFVDVPGFL PGVDQEHDGI IRRGAKLIFA YAEATVPLIT VITRKAFGGA 

       430        440        450        460        470        480 
YDVMGSKHLG ADLNLAWPTA QIAVMGAQGA VNILHRRTIA DAGDDAEATR ARLIQEYEDA 

       490        500        510        520        530 
LLNPYTAAER GYVDAVIMPS DTRRHIVRGL RQLRTKRESL PPKKHGNIPL

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References

[1]	Gramajo H.C., Rodriguez E.J., Danchin A. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: A3 EMBL AAD28194.1.
[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: A3 EMBL AAD28194.1.
[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, 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF113605 Genomic DNA. Translation: AAD28194.1.

PIR

T42208.

RefSeq

NP_629079.1. NC_003888.3.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9X4K7.

SMR

Q9X4K7. Positions 10-530.

ModBase

Search...

Protein-protein interaction databases

STRING

100226.SCO4926.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1100367.

KEGG

sco:SCO4926.

PATRIC

23739690. VBIStrCoe124346_5005.

Phylogenomic databases

HOGENOM

HOG000218693.

KO

K01966.

ProtClustDB

CLSK636053.

Family and domain databases

InterPro

IPR000438. Acetyl_CoA_COase_Trfase_b_su.
IPR000022. Carboxyl_trans.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
[Graphical view]

Pfam

PF01039. Carboxyl_trans. 1 hit.
[Graphical view]

PRINTS

PR01070. ACCCTRFRASEB.

PROSITE

PS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9X4K7.

Entry information

Entry name

Q9X4K7_STRCH

Accession

Primary (citable) accession number: Q9X4K7

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1999
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)