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A1U1Q6 (MASZ_MARAV) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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 attributes

Sequence length726 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

Catalytic activity

Acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA. HAMAP-Rule MF_00641

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00641

Pathway

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

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00641

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00641.

Sequence similarities

Belongs to the malate synthase family. GlcB subfamily.

Ontologies

Keywords
   Biological processGlyoxylate bypass
Tricarboxylic acid cycle
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionTransferase
   PTMOxidation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglyoxylate cycle

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmalate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 726726Malate synthase G HAMAP-Rule MF_00641
PRO_1000130890

Regions

Region125 – 1262Acetyl-CoA binding By similarity
Region457 – 4604Glyoxylate binding By similarity

Sites

Active site3401Proton acceptor By similarity
Active site6321Proton donor By similarity
Metal binding4321Magnesium By similarity
Metal binding4601Magnesium By similarity
Binding site1181Acetyl-CoA; via carbonyl oxygen By similarity
Binding site2761Acetyl-CoA By similarity
Binding site3131Acetyl-CoA By similarity
Binding site3401Glyoxylate By similarity
Binding site4321Glyoxylate By similarity
Binding site5411Acetyl-CoA; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue6181Cysteine sulfenic acid (-SOH) By similarity

Sequences

Sequence LengthMass (Da)Tools
A1U1Q6 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: C283C1C0799B0F19

FASTA72679,629
        10         20         30         40         50         60 
MTERVQVGGI QIAKNLYDFV NNEAIPGTGI EADKFWAEFD KIVNELAPRN RELLLKRDEI 

        70         80         90        100        110        120 
QEKMDTWNRE HKGQKLDMAE YKAFLKDIGY LVDEPADFKI STSNVDPEIA TMAGPQLVVP 

       130        140        150        160        170        180 
VMNARFALNA ANARWGSLYD ALYGTDAISE ENGAEKGRGY NPVRGAKVIE WARNLLDGSA 

       190        200        210        220        230        240 
PLASGSHKDA AKYYIDGGKL AVKLQNGDVT GLKDESGFVG YTGAADAPTG VLLVKNGMHF 

       250        260        270        280        290        300 
EIQIDASHPI GKDDGAHVKD VLMESALTTI MDCEDSVAAV DADDKVVAYK NWLGLMKGDL 

       310        320        330        340        350        360 
EESFEKGGQM MTRRMNGDRT YTGADGSELT LKGRSLLFVR NVGHLMTNPA ILLKDGSEIP 

       370        380        390        400        410        420 
EGLMDGLVTS LIAIHDLKGD GKFQNSTKGS VYIVKPKQHG PEEVAFTNEF FGRVEDALGL 

       430        440        450        460        470        480 
PRFTLKVGIM DEERRTTVNL KACIHAAKER TVFINTGFLD RTGDEIHTSM ELGPFIRKGP 

       490        500        510        520        530        540 
MKQAAWINAY EQWNVDIGLE AGLSGVAQIG KGMWAMPDLM AGMLEAKIGH PKAGANTAWV 

       550        560        570        580        590        600 
PSPTAATLHA THYHQVNVFD VQKELANRQR ASLDDILTVP VMEDPSSLSA EDIQQELDNN 

       610        620        630        640        650        660 
AQGILGYVVR WIDQGVGCSK VPDINDVGLM EDRATLRISS QLLTNWLYHG ICSEEQIMET 

       670        680        690        700        710        720 
MKRMAAVVDK QNAGDAAYRN MAPNFDDSIA FQAAVDLVLK GREQPAGYTE PLLHAYRQKA 


KAKYGQ 

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References

[1]"Complete sequence of chromosome 1 of Marinobacter aquaeolei VT8."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Edwards K., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700491 / DSM 11845 / VT8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000514 Genomic DNA. Translation: ABM18925.1.
RefSeqYP_959112.1. NC_008740.1.

3D structure databases

ProteinModelPortalA1U1Q6.
SMRA1U1Q6. Positions 2-726.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351348.Maqu_1843.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM18925; ABM18925; Maqu_1843.
GeneID4655277.
KEGGmaq:Maqu_1843.
PATRIC22458986. VBIMarAqu65105_2253.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2225.
HOGENOMHOG000220740.
KOK01638.
OMAPKMHGPD.
OrthoDBEOG6HJ286.
ProtClustDBPRK02999.

Enzyme and pathway databases

BioCycMHYD351348:GHYZ-1883-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 nameMASZ_MARAV
AccessionPrimary (citable) accession number: A1U1Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 55 of the entry and version 1 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