Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A7ZRK3 (A7ZRK3_ECO24) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 61. Feed History...

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

Protein attributes

Sequence length723 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Region125 – 1262Acetyl-CoA binding By similarity HAMAP-Rule MF_00641
Region452 – 4554Glyoxylate binding By similarity HAMAP-Rule MF_00641

Sites

Active site3381Proton acceptor By similarity HAMAP-Rule MF_00641
Active site6311Proton donor By similarity HAMAP-Rule MF_00641
Metal binding4271Magnesium By similarity HAMAP-Rule MF_00641
Metal binding4551Magnesium By similarity HAMAP-Rule MF_00641
Binding site1181Acetyl-CoA; via carbonyl oxygen By similarity HAMAP-Rule MF_00641
Binding site2741Acetyl-CoA By similarity HAMAP-Rule MF_00641
Binding site3111Acetyl-CoA By similarity HAMAP-Rule MF_00641
Binding site3381Glyoxylate By similarity HAMAP-Rule MF_00641
Binding site4271Glyoxylate By similarity HAMAP-Rule MF_00641
Binding site5361Acetyl-CoA; via carbonyl oxygen By similarity HAMAP-Rule MF_00641

Amino acid modifications

Modified residue6171Cysteine sulfenic acid (-SOH) By similarity HAMAP-Rule MF_00641
Modified residue6881Cysteine sulfenic acid (-SOH) By similarity HAMAP-Rule MF_00641

Sequences

Sequence LengthMass (Da)Tools
A7ZRK3 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 4B160E959727C3F2

FASTA72380,519
        10         20         30         40         50         60 
MSQTITQGRL RIDANFKRFV DEEVLPGTGQ DAAAFWRNFD EIVHDLAPEN RQLLAERDRI 

        70         80         90        100        110        120 
QAALDEWHRS NPGPVKDKAA YKSFLRELGY LVPQPERVTV ETTGIDSEIT SQAGPQLVVP 

       130        140        150        160        170        180 
AMNARYALNA ANARWGSLYD ALYGSDIIPQ EGAMVSGYDP QRGEQVIAWV RRFLDESLPL 

       190        200        210        220        230        240 
ENGSYQDVVA FKVVDKQLRI QLKNGKETTL RTPAQFVGYR GDAAALTCIL LKNNGLHIEL 

       250        260        270        280        290        300 
QIDANGRIGK DDPAHINDVI VEAAISTILD CEDSVAAVDA EDKILLYRNL LGLMQGTLQE 

       310        320        330        340        350        360 
KMEKNGRQIV RKLNDDRHYT AADGSEISLH GRSLLFIRNV GHLMTIPVIW DSEGNEIPEG 

       370        380        390        400        410        420 
ILDGVMTGAI ALYDLKVQKN SRTGSVYIVK PKMHGPQEVA FANKLFTRIE TMLGMAPNTL 

       430        440        450        460        470        480 
KMGIMDEERR TSLNLRSCIA QARNRVAFIN TGFLDRTGDE MHSVMEAGPM LRKNQMKSTP 

       490        500        510        520        530        540 
WIKAYERNNV LSGLFCGLRG KAQIGKGMWA MPDLMADMYS QKGDQLRAGA NTAWVPSPTA 

       550        560        570        580        590        600 
ATLHALHYHQ TNVQSVQANI AQTEFNAEFE PLLDDLLTIP VAENANWSVE EIQQELDNNV 

       610        620        630        640        650        660 
QGILGYVVRW VEQGIGCSKV PDIHNVALME DRATLRISSQ HIANWLRHGI LTKEQVQASL 

       670        680        690        700        710        720 
ENMAKVVDQQ NAGDPAYRPM AGNFANSCAF KAASDLIFLG VKQPNGYTEP LLHAWRLREK 


ESH 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E24377A / ETEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV18902.1.
RefSeqYP_001464432.1. NC_009801.1.

3D structure databases

ProteinModelPortalA7ZRK3.
SMRA7ZRK3. Positions 1-723.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING331111.EcE24377A_3435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV18902; ABV18902; EcE24377A_3435.
GeneID5590624.
KEGGecw:EcE24377A_3435.
PATRIC18296186. VBIEscCol31211_3708.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2225.
HOGENOMHOG000220740.
KOK01638.
OMAPANTLKM.
OrthoDBEOG6HJ286.

Enzyme and pathway databases

BioCycECOL331111:GH7P-3416-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 nameA7ZRK3_ECO24
AccessionPrimary (citable) accession number: A7ZRK3
Entry history
Integrated into UniProtKB/TrEMBL: October 23, 2007
Last sequence update: October 23, 2007
Last modified: July 9, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)