Beta-ketoacyl synthase - Brucella abortus (strain 2308)

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Q2YQQ9 (Q2YQQ9_BRUA2) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 42. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info Customize order

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Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Submitted name:
Beta-ketoacyl synthase EMBL CAJ12129.1
EC=2.3.1.41 EMBL CAJ12129.1

Gene names

Name:	fabB EMBL CAJ12129.1
Ordered Locus Names:	BAB1_2173

Organism

Brucella abortus (strain 2308) [Complete proteome] [HAMAP]

Taxonomic identifier

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	407 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the beta-ketoacyl-ACP synthases family. RuleBase RU003694

Ontologies

Keywords
Molecular function	Acyltransferase EMBL CAJ12129.1 Transferase
Technical term	3D-structure PDB 3MQD PDB 3LRF Complete proteome
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequences

Sequence

Length

Mass (Da)

Tools

Q2YQQ9 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 26DB912A67F0AD07
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407

43,311

        10         20         30         40         50         60 
MRRVVVTGMG IVSSIGSNTE EVTASLREAK SGISRAEEYA ELGFRCQVHG APDIDIESLV 

        70         80         90        100        110        120 
DRRAMRFHGR GTAWNHIAMD QAIADAGLTE EEVSNERTGI IMGSGGPSTR TIVDSADITR 

       130        140        150        160        170        180 
EKGPKRVGPF AVPKAMSSTA SATLATFFKI KGINYSISSA CATSNHCIGN AYEMIQYGKQ 

       190        200        210        220        230        240 
DRMFAGGCED LDWTLSVLFD AMGAMSSKYN DTPSTASRAY DKNRDGFVIA GGAGVLVLED 

       250        260        270        280        290        300 
LETALARGAK IYGEIVGYGA TSDGYDMVAP SGEGAIRCMK MALSTVTSKI DYINPHATST 

       310        320        330        340        350        360 
PAGDAPEIEA IRQIFGAGDV CPPIAATKSL TGHSLGATGV QEAIYSLLMM QNNFICESAH 

       370        380        390        400 
IEELDPAFAD MPIVRKRIDN VQLNTVLSNS FGFGGTNATL VFQRYQG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole-genome analyses of speciation events in pathogenic Brucellae." Microbial Genomics Group, Lawrence Livermore National Laboratory, and the Genome Analysis Group, Oak Ridge National Laboratory Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E. Infect. Immun. 73:8353-8361(2005) [PubMed: 16299333] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 2308 EMBL CAJ12129.1.
[2]	"Crystal structure of beta-ketoacyl synthase from brucella melitensis with FOL 0758, (1-methyl-1h-indazol-3-yl) methanol." Seattle Structural Genomics Center for Infectious Disease (SSGCID) Abendroth J., Gardberg A., Sankaran B., Staker B. Submitted (APR-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS).
[3]	"CRYSTAL structure of beta-ketoacyl synthase from brucella melitensis." Seattle Structural Genomics Center for Infectious Disease (SSGCID) Abendroth J., Edwards T., Staker B. Submitted (FEB-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AM040264 Genomic DNA. Translation: CAJ12129.1.

RefSeq

YP_415493.1. NC_007618.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LRF	X-ray	1.60	A	1-407	[»]
3MQD	X-ray	1.25	A	1-407	[»]
3U0E	X-ray	1.60	A	1-407	[»]
3U0F	X-ray	1.25	A	1-407	[»]

ProteinModelPortal

SMR

Q2YQQ9. Positions 1-406.

ModBase

Protein-protein interaction databases

STRING

Protocols and materials databases

StructuralBiologyKnowledgebase

Genome annotation databases

GeneID

GenomeReviews

Gene locus BAB1_2173 in contig AM040264_GR.

KEGG

PATRIC

17847453. VBIBruMel86222_2262.

Organism-specific databases

CMR

Phylogenomic databases

eggNOG

HOGENOM

OMA

ProtClustDB

Family and domain databases

InterPro

IPR000794. Beta-ketoacyl_synthase.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]

Gene3D

G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.

KO

PANTHER

PTHR11712. Ketoacyl_synth. 1 hit.

Pfam

PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]

SUPFAM

SSF53901. Thiolase-like. 2 hits.

PROSITE

PS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]

ProtoNet

Entry information

Entry name

Q2YQQ9_BRUA2

Accession

Primary (citable) accession number: Q2YQQ9

Entry history

Integrated into UniProtKB/TrEMBL:	February 7, 2006
Last sequence update:	February 7, 2006
Last modified:	January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info