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F0L309 (F0L309_AGRSH) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 22. Feed History...

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

Sequence length722 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA By similarity. HAMAP-Rule MF_00641 SAAS SAAS023310

Catalytic activity

Acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA. RuleBase RU003572 HAMAP-Rule MF_00641 SAAS SAAS023310

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00641

Pathway

Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2. RuleBase RU003572 HAMAP-Rule MF_00641 SAAS SAAS023310

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00641

Subcellular location

Cytoplasm By similarity RuleBase RU003572 HAMAP-Rule MF_00641 SAAS SAAS023310.

Sequence similarities

Belongs to the malate synthase family. GlcB subfamily. RuleBase RU003572 HAMAP-Rule MF_00641

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region123 – 1242Acetyl-CoA binding By similarity HAMAP-Rule MF_00641
Region454 – 4574Glyoxylate binding By similarity HAMAP-Rule MF_00641

Sites

Active site3371Proton acceptor By similarity HAMAP-Rule MF_00641
Active site6281Proton donor By similarity HAMAP-Rule MF_00641
Metal binding4291Magnesium By similarity HAMAP-Rule MF_00641
Metal binding4571Magnesium By similarity HAMAP-Rule MF_00641
Binding site1161Acetyl-CoA; via carbonyl oxygen By similarity HAMAP-Rule MF_00641
Binding site2731Acetyl-CoA By similarity HAMAP-Rule MF_00641
Binding site3101Acetyl-CoA By similarity HAMAP-Rule MF_00641
Binding site3371Glyoxylate By similarity HAMAP-Rule MF_00641
Binding site4291Glyoxylate By similarity HAMAP-Rule MF_00641
Binding site5381Acetyl-CoA; via carbonyl oxygen By similarity HAMAP-Rule MF_00641

Amino acid modifications

Modified residue6141Cysteine sulfenic acid (-SOH) By similarity HAMAP-Rule MF_00641

Sequences

Sequence LengthMass (Da)Tools
F0L309 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 9786A22B45A57D54

FASTA72278,710
        10         20         30         40         50         60 
MSRTNKFGLS IDDRLYAFLT DDVLPGTGFD AETFFEGFSA IVHELSPKNR ELLEKRDALQ 

        70         80         90        100        110        120 
EKLDGWYRQN GAPTDFDVYE GFLKEIGYLL PEGPGFKVET SNVDSEIAAV AGPQLVVPVM 

       130        140        150        160        170        180 
NARYALNAAN ARWGSLYDAL YGTDAISDAD GAEKGRGYNP KRGEKVIAWA RNFLNESAPL 

       190        200        210        220        230        240 
ETAGWSDVTG FKIVDGLLQL AIGDSKTGLK DAEQFKGFTG DAEKPATILL GKNGLHTEIV 

       250        260        270        280        290        300 
IDPSTEIGKG DKAGISDVIL ESALTTIMDC EDSVAAVDAE DKVLVYGNWL GLMRGDLTEK 

       310        320        330        340        350        360 
VSKGGNTFTR SLNPDRYYTA PDGGALTLPG RSLMLVRNVG HLMTNPAILD KDGREVPEGI 

       370        380        390        400        410        420 
MDAVVTALIA LYDVGPSGRR QNSRAGSMYV VKPKMHGPEE VAFANEIFTR AEKLVGMAPN 

       430        440        450        460        470        480 
TMKMGIMDEE RRTTVNLKES IRAAKDRVVF INTGFLDRTG DEIHTSMEAG PMIRKGDMKQ 

       490        500        510        520        530        540 
AAWIAAYENW NVDIGLECGL SGNAQIGKGM WAMPDLMAAM LEQKIAHPKA GANTAWVPSP 

       550        560        570        580        590        600 
TAATLHATHY HKVDVAAVQD DLKSRGRAKL SDILSVPVVP RPNWTPEEIQ RELDNNAQGI 

       610        620        630        640        650        660 
LGYVVRWVDQ GVGCSKVPDI NNVGLMEDRA TLRISAQHMA NWLRHGVVTQ EQIVETMKRM 

       670        680        690        700        710        720 
AAVVDSQNAG DPAYLPMASN FEGSVAFQAA VELVLKGREQ PNGYTEPVLH RRRLELKAKQ 


AA 

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References

[1]"Complete genome sequencing of Agrobacterium sp H13-3, the former Rhizobium lupini H13-3, reveals a tripartite genome consisting of a circular and a linear chromosome and an accessory plasmid but lacking a tumor-inducing Ti-plasmid."
Wibberg D., Blom J., Jaenicke S., Kollin F., Rupp O., Scharf B., Schneiker-Bekel S., Sczcepanowski R., Goesmann A., Setubal J.C., Schmitt R., Puhler A., Schluter A.
J. Biotechnol. 155:50-62(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: H13-3 EMBL ADY63045.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002248 Genomic DNA. Translation: ADY63045.1.
RefSeqYP_004277365.1. NC_015183.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADY63045; ADY63045; AGROH133_02861.
GeneID10265805.
KEGGagr:AGROH133_02861.
PATRIC46844791. VBIAgrSp164909_0047.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01638.
OMAPKMHGPD.

Enzyme and pathway databases

BioCycASP861208:GH59-48-MONOMER.
UniPathwayUPA00703; UER00720.

Family and domain databases

Gene3D2.170.170.11. 2 hits.
HAMAPMF_00641. Malate_synth_G.
InterProIPR011076. Malate_synth-like.
IPR023310. Malate_synth_G_beta_sub_dom.
IPR001465. Malate_synthase.
IPR006253. Malate_synthG.
[Graphical view]
PfamPF01274. Malate_synthase. 1 hit.
[Graphical view]
SUPFAMSSF51645. SSF51645. 1 hit.
TIGRFAMsTIGR01345. malate_syn_G. 1 hit.
ProtoNetSearch...

Entry information

Entry nameF0L309_AGRSH
AccessionPrimary (citable) accession number: F0L309
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: February 19, 2014
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)