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H2FUS5 (H2FUS5_OCESG) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 9. 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:
8-amino-7-oxononanoate synthase HAMAP-Rule MF_01693
Short name=AONS HAMAP-Rule MF_01693
EC=2.3.1.47 HAMAP-Rule MF_01693
Alternative name(s):
7-keto-8-amino-pelargonic acid synthase HAMAP-Rule MF_01693
8-amino-7-ketopelargonate synthase HAMAP-Rule MF_01693
L-alanine--pimeloyl-CoA ligase HAMAP-Rule MF_01693
Gene names
Name:bioF HAMAP-Rule MF_01693
Ordered Locus Names:GU3_09025 EMBL AEY01561.1
OrganismOceanimonas sp. (strain GK1) [Complete proteome] [HAMAP] EMBL AEY01561.1
Taxonomic identifier511062 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Oceanimonas

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the decarboxylative condensation of pimeloyl-CoA and L-alanine to produce 8-amino-7-oxononanoate (AON), coenzyme A, and carbon dioxide By similarity. SAAS SAAS004723 HAMAP-Rule MF_01693

Catalytic activity

6-carboxyhexanoyl-CoA + L-alanine = 8-amino-7-oxononanoate + CoA + CO2. SAAS SAAS004723 HAMAP-Rule MF_01693

Cofactor

Pyridoxal phosphate By similarity. SAAS SAAS004723 HAMAP-Rule MF_01693

Pathway

Cofactor biosynthesis; biotin biosynthesis; 8-amino-7-oxononanoate from pimeloyl-CoA: step 1/1. SAAS SAAS004723 HAMAP-Rule MF_01693

Subunit structure

Homodimer By similarity. SAAS SAAS004723 HAMAP-Rule MF_01693

Sequence similarities

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily. HAMAP-Rule MF_01693

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region104 – 1052Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01693
Region197 – 2004Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01693
Region229 – 2324Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01693

Sites

Binding site171Substrate By similarity HAMAP-Rule MF_01693
Binding site1291Substrate By similarity HAMAP-Rule MF_01693
Binding site1721Pyridoxal phosphate By similarity HAMAP-Rule MF_01693
Binding site3461Substrate By similarity HAMAP-Rule MF_01693

Amino acid modifications

Modified residue2321N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01693

Sequences

Sequence LengthMass (Da)Tools
H2FUS5 [UniParc].

Last modified March 21, 2012. Version 1.
Checksum: A32A9CB1681E3E64

FASTA38240,474
        10         20         30         40         50         60 
MPFNLSLAER DAAGLKRTLP AIDRVDGRWL HAGGQTYLNF AGNDYLGLSR APELRAAAEQ 

        70         80         90        100        110        120 
AAREFGVGAV ASPLVVGHQA IHRELEEELC DWLGLEAVML FSSGFSANQA VIKALLGKEH 

       130        140        150        160        170        180 
TLWQDRLNHA SLQEAGLLSP ARMVRFAHND MAALAAKLKP SAGLIISEGV FSMDGDTAPW 

       190        200        210        220        230        240 
PELVRLASAS GNWLMIDDAH GLGVLGQEGR GTLNEQGLEA GSVNIFMGTF GKALGVSGAF 

       250        260        270        280        290        300 
VGGSRALVEY LHNLGRSYIY STHLPPPQAA AVLAAVRLVR QADDKRAHLR ELVSQFRAGV 

       310        320        330        340        350        360 
ADLPLQLLPS ATAIQPLVVG EEAATLSLAA ALKQQGLWTG AIRPPTVPKG SARLRITLSA 

       370        380 
AHTQADVQRL IDALHGACSP SP

« Hide

References

[1]"Complete genome sequence of Oceanimonas sp. GK1, a halotolerant bacterium from Gavkhouni Wetland in Iran."
Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., Ramezani M., Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.
J. Bacteriol. 194:2123-2124(2012)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GK1 EMBL AEY01561.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP003171 Genomic DNA. Translation: AEY01561.1.
RefSeqYP_005092311.1. NC_016745.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEY01561; AEY01561; GU3_09025.
GeneID11599942.
KEGGoce:GU3_09025.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00652.

Enzyme and pathway databases

UniPathwayUPA00078; UER00159.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01693. BioF_aminotrans_2.
InterProIPR022834. Amino_oxononanoate_synth.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR004723. BioF.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR00858. bioF. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameH2FUS5_OCESG
AccessionPrimary (citable) accession number: H2FUS5
Entry history
Integrated into UniProtKB/TrEMBL: March 21, 2012
Last sequence update: March 21, 2012
Last modified: April 3, 2013
This is version 9 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info