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Protein

2-methylisocitrate lyase

Gene

prpB

Organism
Bacillus anthracis
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate.UniRule annotation
Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle (propionate degradation route). Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via an alpha-carboxy-carbanion intermediate.UniRule annotation

Catalytic activityi

(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate.UniRule annotation

Cofactori

Mg2+UniRule annotation

Pathwayi: propanoate degradation

This protein is involved in the pathway propanoate degradation, which is part of Organic acid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway propanoate degradation and in Organic acid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531Pyruvate 2Combined sources
Metal bindingi92 – 921MagnesiumUniRule annotation
Binding sitei92 – 921Pyruvate 1Combined sources
Metal bindingi94 – 941MagnesiumUniRule annotation
Binding sitei162 – 1621SubstrateUniRule annotation
Binding sitei192 – 1921SubstrateUniRule annotation
Binding sitei224 – 2241Pyruvate 6Combined sources
Binding sitei245 – 2451SubstrateUniRule annotation
Binding sitei274 – 2741SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationImported

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation, PyruvateCombined sources

Enzyme and pathway databases

BioCyciBANT260799:GJAJ-2256-MONOMER.
BANT261594:GJ7F-2334-MONOMER.
UniPathwayiUPA00946.

Names & Taxonomyi

Protein namesi
Recommended name:
2-methylisocitrate lyaseUniRule annotation (EC:4.1.3.30UniRule annotation)
Short name:
2-MICUniRule annotation
Short name:
MICLUniRule annotation
Alternative name(s):
(2R,3S)-2-methylisocitrate lyaseUniRule annotation
Gene namesi
Name:prpBUniRule annotationImported
Ordered Locus Names:GBAA_2350Imported
ORF Names:AB893_11655Imported, BASH2_03522Imported
OrganismiBacillus anthracisImported
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi198094.BA_2350.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IQDX-ray2.00A/B1-302[»]
4IQEX-ray2.50A/B1-302[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 533Pyruvate 1 bindingCombined sources
Regioni53 – 553Substrate bindingUniRule annotation
Regioni76 – 772Pyruvate 4 bindingCombined sources
Regioni77 – 804Pyruvate 3 bindingCombined sources
Regioni129 – 1302Substrate bindingUniRule annotation
Regioni214 – 2163Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the isocitrate lyase/PEP mutase superfamily. Methylisocitrate lyase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG2513. LUCA.
HOGENOMiHOG000220041.
KOiK03417.
OMAiFGQTELW.
OrthoDBiEOG6BGP03.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
HAMAPiMF_01939. PrpB.
InterProiIPR018523. Isocitrate_lyase_ph_CS.
IPR012695. PrpB.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR02317. prpB. 1 hit.
PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q81QR8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWVVNKQST QEELANRFRA LVEANEILQI PGAHDAMAAL VARNTGFLAL
60 70 80 90 100
YLSGAAYTAS KGLPDLGIVT STEVAERARD LVRATDLPVL VDIDTGFGGV
110 120 130 140 150
LNVARTAVEM VEAKVAAVQI EDQQLPKKCG HLNGKKLVTT EELVQKIKAI
160 170 180 190 200
KEVAPSLYIV ARTDARGVEG LDEAIERANA YVKAGADAIF PEALQSEEEF
210 220 230 240 250
RLFNSKVNAP LLANMTEFGK TPYYSAEEFA NMGFQMVIYP VTSLRVAAKA
260 270 280 290 300
YENVFTLIKE TGSQKDALSN MQTRSELYET ISYHDFEELD TGIAKTVLSE

DQ
Length:302
Mass (Da):33,016
Last modified:June 1, 2003 - v1
Checksum:iFFCD10E8A9CB1F7B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017334 Genomic DNA. Translation: AAT31469.1.
CP012519 Genomic DNA. Translation: ALC34465.1.
AP014833 Genomic DNA. Translation: BAR76929.1.
RefSeqiWP_000312652.1. NZ_LHUO01000023.1.

Genome annotation databases

EnsemblBacteriaiAAT31469; AAT31469; GBAA_2350.
AJG29064; AJG29064; TM00_11670.
AJH86176; AJH86176; BF27_5227.
KEGGibanh:HYU01_11705.
bar:GBAA_2350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017334 Genomic DNA. Translation: AAT31469.1.
CP012519 Genomic DNA. Translation: ALC34465.1.
AP014833 Genomic DNA. Translation: BAR76929.1.
RefSeqiWP_000312652.1. NZ_LHUO01000023.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IQDX-ray2.00A/B1-302[»]
4IQEX-ray2.50A/B1-302[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198094.BA_2350.

Protocols and materials databases

DNASUi1089117.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT31469; AAT31469; GBAA_2350.
AJG29064; AJG29064; TM00_11670.
AJH86176; AJH86176; BF27_5227.
KEGGibanh:HYU01_11705.
bar:GBAA_2350.

Phylogenomic databases

eggNOGiCOG2513. LUCA.
HOGENOMiHOG000220041.
KOiK03417.
OMAiFGQTELW.
OrthoDBiEOG6BGP03.

Enzyme and pathway databases

UniPathwayiUPA00946.
BioCyciBANT260799:GJAJ-2256-MONOMER.
BANT261594:GJ7F-2334-MONOMER.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
HAMAPiMF_01939. PrpB.
InterProiIPR018523. Isocitrate_lyase_ph_CS.
IPR012695. PrpB.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR02317. prpB. 1 hit.
PROSITEiPS00161. ISOCITRATE_LYASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames AncestorImported and Ames ancestorImported.
  2. "Crystal Structure of Carboxyvinyl-Carboxyphosphonate Phosphorylmutase from Bacillus anthracis str. Ames Ancestor."
    Center for Structural Genomics of Infectious Diseases (CSGID)
    Kim Y., Maltseva N., Kwon K., Anderson W.F., Joachimiak A.
    Submitted (JAN-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
  3. "Crystal Structure of Carboxyvinyl-Carboxyphosphonate Phosphorylmutase from Bacillus anthracis."
    Center for Structural Genomics of Infectious Diseases (CSGID)
    Kim Y., Maltseva N., Kwon K., Anderson W.F., Joachimiak A.
    Submitted (JAN-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH PYRUVATE.
  4. "Bacillus anthracis whole genome sequence."
    Okutani A., Morikawa S., Inoue S.
    Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Shikan-NIIDImported.
  5. "Draft genome sequence of Bacillus anthracis Larissa associated with a case of cutaneous anthrax in Greece."
    Grass G., Hanczaruk M., Antwerpen M.H.
    Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: LarissaImported.

Entry informationi

Entry nameiQ81QR8_BACAN
AccessioniPrimary (citable) accession number: Q81QR8
Secondary accession number(s): E9R2D6
, E9R2D7, Q6HYY7, Q6KSY6
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2003
Last sequence update: June 1, 2003
Last modified: April 13, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.