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B2HNJ0 (PLSB_MYCMM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glycerol-3-phosphate acyltransferase

Short name=GPAT
EC=2.3.1.15
Gene names
Name:plsB
Ordered Locus Names:MMAR_3833
OrganismMycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP]
Taxonomic identifier216594 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length788 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate. HAMAP MF_00393

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. HAMAP MF_00393

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity HAMAP MF_00393.

Domain

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity. HAMAP MF_00393

Sequence similarities

Belongs to the GPAT/DAPAT family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentCell membrane
Membrane
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglycerol-3-phosphate O-acyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 788788Glycerol-3-phosphate acyltransferase HAMAP MF_00393
PRO_1000123085

Regions

Motif271 – 2766HXXXXD motif HAMAP MF_00393

Sequences

Sequence LengthMass (Da)Tools
B2HNJ0 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 4367AF048DA614E3

FASTA78888,236
        10         20         30         40         50         60 
MTKPVADTSA VLTSEDTLVL ASMGSPVEMQ LIMDWLGEQR ARTPGAKFDV LKLPPRNAPT 

        70         80         90        100        110        120 
AALTALVEQL ESGSEAGADR SIVPVQVFWQ PPADRSRLAK VAGLLPGRDP YHPNPRQQRR 

       130        140        150        160        170        180 
ILRSDPQRAR VMAGESATVS ELRKQWRDNT VGEDQHDFAH FVARRAILAL ARAEYRILGP 

       190        200        210        220        230        240 
QYKSPRLVKP EMLASARFRA GLEKIPGATV EEAGKMLDEL ATGWSQASVD VFSVLGRLIS 

       250        260        270        280        290        300 
RGFDPEFDYD EYQVAAMRTA LEAHPAVLLF SHRSYIDGAV VPVAMQDNRL PPVHMFGGVN 

       310        320        330        340        350        360 
LSFGVMGPLM RRAGMIFIRR NIAGDPLYKY VLKEYVGYVV EKRFNLSWSI EGTRSRTGKM 

       370        380        390        400        410        420 
LPPKLGLMSY VADAYLDGRS DDILLQGVSI CFDQLHEIAE YAAYARGAEK TPEGFSWLYN 

       430        440        450        460        470        480 
FIKAQGERNY GKIYVRFPEA VSMRQYLGVP HGPITHDLAA KRLALQKMSF EVAWRILRAT 

       490        500        510        520        530        540 
PMTATGLVCA LLLTARGTAL TLGQLHHTLQ DSLDYLERKQ TPMSTSALRL RSREGVRAAV 

       550        560        570        580        590        600 
DALSNAHPVT RVDSGREPVW YIAPEDELAA AFYRNSVIHA FLETSIVELA LAHARHAEGD 

       610        620        630        640        650        660 
RMAAFWDQVM RLRDLLKFDF YFADSAAFRA NIAEEMAWHR DWESQVAAGG DQIDAILYAK 

       670        680        690        700        710        720 
RPLISDAMLR VFFEAYAIVA DVLRDAPANI KQKDLTDLAL GLGRQYVAQA RVRSSEPVST 

       730        740        750        760        770        780 
LLFATARQVV DDQHLIEPAP DLTERRSAFL AELRNILRDF DYVGKIARNR FVARELKARQ 


ERLEQQAQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000854 Genomic DNA. Translation: ACC42243.1.
RefSeqYP_001852098.1. NC_010612.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB2HNJ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000035281; EBMYCP00000033721; EBMYCG00000035276.
GeneID6228107.
GenomeReviewsGene locus MMAR_3833 in contig CP000854_GR.
KEGGmmi:MMAR_3833.
PATRIC18068865. VBIMycMar75906_4107.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000018019.
HOGENOMHBG565163.
OMAIVPVAMQ.
ProtClustDBPRK03355.

Family and domain databases

HAMAPMF_00393. Glyc3P_acyltrans.
[Tree]
InterProIPR002123. Acyltransferase.
IPR022284. G3P_O-AcylTrfase.
[Graphical view]
KOK00631.
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFPIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLSB_MYCMM
AccessionPrimary (citable) accession number: B2HNJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: January 25, 2012
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families