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P71534 (FABG_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] reductase FabG

EC=1.1.1.100
Alternative name(s):
3-ketoacyl-acyl carrier protein reductase
Beta-Ketoacyl-acyl carrier protein reductase
Beta-ketoacyl-ACP reductase
Gene names
Name:fabG
Ordered Locus Names:MSMEG_3150, MSMEI_3069
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis By similarity.

Catalytic activity

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Sequence caution

The sequence AFP39533.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2552553-oxoacyl-[acyl-carrier-protein] reductase FabG
PRO_0000054674

Regions

Nucleotide binding30 – 334NADP By similarity
Nucleotide binding69 – 702NADP By similarity
Nucleotide binding161 – 1655NADP By similarity

Sites

Active site1611Proton acceptor By similarity
Binding site551NADP By similarity
Binding site961NADP; via carbonyl oxygen By similarity
Binding site1481Substrate By similarity
Binding site1941NADP; via amide nitrogen and carbonyl oxygen By similarity

Experimental info

Sequence conflict751A → G in AAC69638. Ref.1
Sequence conflict1801A → D in AAC69638. Ref.1
Sequence conflict189 – 1902VA → LP in AAC69638. Ref.1
Sequence conflict2081A → G in AAC69638. Ref.1
Sequence conflict2111L → I in AAC69638. Ref.1
Sequence conflict2161A → D in AAC69638. Ref.1
Sequence conflict2221A → V in AAC69638. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P71534 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: BAE0131C09C472DB

FASTA25526,641
        10         20         30         40         50         60 
MTVTDNPADT AGEATAGRPA FVSRSVLVTG GNRGIGLAIA RRLAADGHKV AVTHRGSGAP 

        70         80         90        100        110        120 
DDLFGVQCDV TDSAAVDRAF KEVEEHQGPV EVLVANAGIS KDAFLMRMTE ERFEEVINTN 

       130        140        150        160        170        180 
LTGAFRCAQR ASRTMQRKRF GRIIFIGSVS GMWGIGNQAN YAAAKAGLIG MARSISRELA 

       190        200        210        220        230        240 
KAGVTANVVA PGYIDTEMTR ALDERIQAGA LDFIPAKRVG TAEEVAGAVS FLASEDASYI 

       250 
AGAVIPVDGG MGMGH 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, expression and characterization of 3-ketoacyl reductase from mycobacteria."
Banerjee A., Sugantino M., Sacchettini J.C., Jacobs W.R. Jr.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[3]"Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[4]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U66800 Genomic DNA. Translation: AAC69638.1.
CP000480 Genomic DNA. Translation: ABK71816.1.
CP001663 Genomic DNA. Translation: AFP39533.1. Different initiation.
RefSeqYP_006567828.1. NC_018289.1.
YP_887465.1. NC_008596.1.

3D structure databases

ProteinModelPortalP71534.
SMRP71534. Positions 17-255.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246196.MSMEG_3150.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK71816; ABK71816; MSMEG_3150.
AFP39533; AFP39533; MSMEI_3069.
GeneID13425436.
4534094.
KEGGmsg:MSMEI_3069.
msm:MSMEG_3150.
PATRIC18078726. VBIMycSme59918_3111.

Phylogenomic databases

eggNOGCOG1028.
KOK11610.
OMADTATENT.
OrthoDBEOG6N3CR8.
ProtClustDBCLSK871938.

Enzyme and pathway databases

BioCycMSME246196:GJ4Y-3150-MONOMER.
UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFABG_MYCS2
AccessionPrimary (citable) accession number: P71534
Secondary accession number(s): A0QX27, I7FLD4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 10, 2007
Last modified: November 13, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways