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F6INB4 (F6INB4_9SPHN) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 18. 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

Names and origin

Protein attributes

Sequence length704 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 SAAS006253

Catalytic activity

Acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA. RuleBase RU003572 HAMAP-Rule MF_00641 SAAS SAAS006253

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 SAAS006253

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00641

Subcellular location

Cytoplasm By similarity RuleBase RU003572 HAMAP-Rule MF_00641 SAAS SAAS006253.

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
Region435 – 4384Glyoxylate binding By similarity HAMAP-Rule MF_00641

Sites

Active site3181Proton acceptor By similarity HAMAP-Rule MF_00641
Active site6091Proton donor By similarity HAMAP-Rule MF_00641
Metal binding4101Magnesium By similarity HAMAP-Rule MF_00641
Metal binding4381Magnesium By similarity HAMAP-Rule MF_00641
Binding site1181Acetyl-CoA; via carbonyl oxygen By similarity HAMAP-Rule MF_00641
Binding site2541Acetyl-CoA By similarity HAMAP-Rule MF_00641
Binding site2911Acetyl-CoA By similarity HAMAP-Rule MF_00641
Binding site3181Glyoxylate By similarity HAMAP-Rule MF_00641
Binding site4101Glyoxylate By similarity HAMAP-Rule MF_00641
Binding site5191Acetyl-CoA; via carbonyl oxygen By similarity HAMAP-Rule MF_00641

Amino acid modifications

Modified residue5951Cysteine sulfenic acid (-SOH) By similarity HAMAP-Rule MF_00641

Sequences

Sequence LengthMass (Da)Tools
F6INB4 [UniParc].

Last modified July 27, 2011. Version 1.
Checksum: CDA840251055D982

FASTA70476,484
        10         20         30         40         50         60 
MTQRVERSGL QIDAGLAAFV EEKVLAPIGQ DTDAFWSGFA QLLARFAPRN RELLEKRDHL 

        70         80         90        100        110        120 
QSQIDAWHMS RAGRPIEQGE YQAFLQDIGY LVPEPEVFSI GTRNVDPEIA TMAGPQLVVP 

       130        140        150        160        170        180 
VLNARFLLNA ANARWGSLYD AFYGTDALDA APAQGKGYDP VRGAAVIAEG RKFLDKALPL 

       190        200        210        220        230        240 
ASGSWADVDS LEVTLVDPDQ CVGETRKGCL FKSNGLHIEI VVDPSSQVGA TDKAGISDIV 

       250        260        270        280        290        300 
LEAALTTIVD LEDSVAAVDA EDKLLAYSNW LGVIRGDLTD TFEKGGQTLT RELAGNKVVT 

       310        320        330        340        350        360 
VPTGEAQELP GRSLLFVRNV GHLMTNPAIL LPDGSEIPEG IMDAVITSAI SAQDVKGMTR 

       370        380        390        400        410        420 
YGNSRKGSIY IVKPKMHGPE ECSFTNDLFD AVEDLLQLPR NTVKVGVMDE ERRTSANLAA 

       430        440        450        460        470        480 
CIHAVKDRIV FINTGFLDRT GDEIHTSMRA GPMIRKSAIK GSTWIAAYEK RNVAIGLRHG 

       490        500        510        520        530        540 
LSGVAQIGKG MWAAPDMMRD MMEQKVGHPR TGANTAWVPS PTAATLHAMH YHEVDVFGLR 

       550        560        570        580        590        600 
EGIAAEEIPG LDLLLQIPLA DGANWSEDEV REELENNAQG LLGYVVRWID QGVGCSKVPD 

       610        620        630        640        650        660 
INDVGLMEDR ATLRISSQHM ANWLLHGVCT EAQVMDALKR MAEKVDAQNA GDPLYAPMAG 

       670        680        690        700 
NWDTSLAFKA ACDLVFKGVE QPSGYTEPLL HAWRLKKKSA LVTA 

« Hide

References

[1]"De Novo Sequencing and Assembly of the Whole Genome of Novosphingobium sp. Strain PP1Y."
D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L., Notomista E., Paolella G., Di Donato A., Salvatore F.
J. Bacteriol. 193:4296-4296(2011)
Cited for: NUCLEOTIDE SEQUENCE.
Strain: PP1Y EMBL CCA92916.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FR856862 Genomic DNA. Translation: CCA92916.1.
RefSeqYP_004534734.1. NC_015580.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCA92916; CCA92916; PP1Y_AT20390.
GeneID10715386.
KEGGnpp:PP1Y_AT20390.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01638.

Enzyme and pathway databases

BioCycNSP702113:GJD2-1971-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 nameF6INB4_9SPHN
AccessionPrimary (citable) accession number: F6INB4
Entry history
Integrated into UniProtKB/TrEMBL: July 27, 2011
Last sequence update: July 27, 2011
Last modified: February 19, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)