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A4SGC2 (A4SGC2_PROVI) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell By similarity. SAAS SAAS003835

Catalytic activity

UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate = UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate. SAAS SAAS003835

Pathway

Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 5/6. SAAS SAAS003835

Sequences

Sequence LengthMass (Da)Tools
A4SGC2 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 34483DA417C1DD59

FASTA39343,207
        10         20         30         40         50         60 
MPKKLFVLAG EVSGDMHAAP AVARLVQEVP GLRVFGVGGE GLRRLGAELL YDTGQMSIMG 

        70         80         90        100        110        120 
FFDVLKHAGF LRRVIRDLKA AVRREMPDAV LLVDYPGMNL IMAKFCRELG IPVIYYISPQ 

       130        140        150        160        170        180 
VWAWKEGRVK AIGASIDRLL VIFRFEVDFF RKHGIDAEFV GHPVIEELSE VQLPPKEAFL 

       190        200        210        220        230        240 
RAHGIGADAQ LVGLLPGSRK QEVSHIFPGM LKGARLLVGG RRVVFLMGRA PNLDGVVYRE 

       250        260        270        280        290        300 
LEEYRDLRIV ECSAYEVMQY SDLGLVTSGT ATLEALCFGM PMVVLYRTGW LNYMIGRMVV 

       310        320        330        340        350        360 
KLTSISLANI VAKGLGAKQQ AVPELIQDAA DGKGIFREAS RILDDPALAA AMRAELLEAR 

       370        380        390 
AGLASESPSR RVAEVVEEYL VGTGRRGALK IKE 

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References

[1]"Complete sequence of Prosthecochloris vibrioformis DSM 265."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., Schuster S.C., Bryant D.A., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 265.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000607 Genomic DNA. Translation: ABP37531.1.
RefSeqYP_001131033.1. NC_009337.1.

3D structure databases

ProteinModelPortalA4SGC2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4SGC2.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4971059.
GenomeReviewsGene locus Cvib_1520 in contig CP000607_GR.
KEGGpvi:Cvib_1520.
PATRIC21397548. VBIChlPha132153_1599.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHBG584837.
OMAPDFNLGL.
PhylomeDBA4SGC2.
ProtClustDBCLSK637261.

Family and domain databases

InterProIPR003835. Glyco_trans_19.
[Graphical view]
KOK00748.
PfamPF02684. LpxB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00215. LpxB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA4SGC2_PROVI
AccessionPrimary (citable) accession number: A4SGC2
Entry history
Integrated into UniProtKB/TrEMBL: May 15, 2007
Last sequence update: May 15, 2007
Last modified: December 14, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)