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Q5FNM2 (Q5FNM2_GLUOX) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 66. 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 attributes

Sequence length468 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH. RuleBase RU003692

Cofactor

Binds 1 FAD per subunit By similarity. RuleBase RU003692

Miscellaneous

The active site is a redox-active disulfide bond By similarity. RuleBase RU003692

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. RuleBase RU003691

Sequences

Sequence LengthMass (Da)Tools
Q5FNM2 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 475199B0B0FC0B3C

FASTA46849,242
        10         20         30         40         50         60 
MCDTFDLIVV GGGPGGYVAA LRASQLGMSV ALVESTHFGG VCLNWGCIPT KALLRSSEIH 

        70         80         90        100        110        120 
HLLHELGTFG LSADNISFDL SKIVGRSRSI ARRMGGGIAH LLKKTKVTTF DGRAKLAGRS 

       130        140        150        160        170        180 
GEAHQVAITK DGAAVATIKA PHVILATGAR GRQLPGLETD GTLIWGAREA MTPKELPKRL 

       190        200        210        220        230        240 
LVIGSGAIGI EFASFYRNMG SEVTIAEVAD RILIAEDPEI SAAARKAFEK QGMKIITSAK 

       250        260        270        280        290        300 
VGPLNKGENE VSTTIESPTG KVDLTVDRVI CAVGIVGNVE DLGLEGTKVQ VERTHIVTDG 

       310        320        330        340        350        360 
FCRTGEPGIY AIGDVAGAPW LAHKASHEGI LCVEKIAGRS PQPLHPLNIP GCTYSRPQIA 

       370        380        390        400        410        420 
SVGLSEEKAI AAGHKVKVGR FPFIANGKAV AMGETDGMVK TVFDATSGEL LGAHMIGAEV 

       430        440        450        460 
TEMIQGYVIT RTGELTEAEL VETVFPHPTI SETMHEATLA AFDGPLHI 

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References

[1]"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
Nat. Biotechnol. 23:195-200(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 621H EMBL AAW62025.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000009 Genomic DNA. Translation: AAW62025.1.
RefSeqYP_192681.1. NC_006677.1.

3D structure databases

ProteinModelPortalQ5FNM2.
ModBaseSearch...

Protein-protein interaction databases

STRING290633.GOX2292.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW62025; AAW62025; GOX2292.
GeneID3249911.
KEGGgox:GOX2292.
PATRIC32612550. VBIGluOxy81109_2608.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000276708.
KOK00382.
OMACTAKIAG.

Enzyme and pathway databases

BioCycGOXY290633:GHB3-2293-MONOMER.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
TIGRFAMsTIGR01350. lipoamide_DH. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ5FNM2_GLUOX
AccessionPrimary (citable) accession number: Q5FNM2
Entry history
Integrated into UniProtKB/TrEMBL: March 1, 2005
Last sequence update: March 1, 2005
Last modified: May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)