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Protein

3-methyl-2-oxobutanoate hydroxymethyltransferase

Gene

panB

Organism
Anabaena variabilis (strain ATCC 29413 / PCC 7937)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate.UniRule annotation

Catalytic activityi

5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = tetrahydrofolate + 2-dehydropantoate.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Pathwayi: (R)-pantothenate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (R)-pantoate from 3-methyl-2-oxobutanoate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 3-methyl-2-oxobutanoate hydroxymethyltransferase (panB)
  2. 2-dehydropantoate 2-reductase (Ava_2981)
This subpathway is part of the pathway (R)-pantothenate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-pantoate from 3-methyl-2-oxobutanoate, the pathway (R)-pantothenate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi44 – 441MagnesiumUniRule annotation
Metal bindingi82 – 821MagnesiumUniRule annotation
Binding sitei82 – 821Alpha-ketoisovalerateUniRule annotation
Binding sitei112 – 1121Alpha-ketoisovalerateUniRule annotation
Metal bindingi114 – 1141MagnesiumUniRule annotation
Active sitei181 – 1811Proton acceptorUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciAVAR240292:GCY3-3957-MONOMER.
UniPathwayiUPA00028; UER00003.

Names & Taxonomyi

Protein namesi
Recommended name:
3-methyl-2-oxobutanoate hydroxymethyltransferaseUniRule annotation (EC:2.1.2.11UniRule annotation)
Alternative name(s):
Ketopantoate hydroxymethyltransferaseUniRule annotation
Short name:
KPHMTUniRule annotation
Gene namesi
Name:panBUniRule annotation
Ordered Locus Names:Ava_3909
OrganismiAnabaena variabilis (strain ATCC 29413 / PCC 7937)
Taxonomic identifieri240292 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena
Proteomesi
  • UP000002533 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2572573-methyl-2-oxobutanoate hydroxymethyltransferasePRO_0000297213Add
BLAST

Interactioni

Subunit structurei

Homodecamer; pentamer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi240292.Ava_3909.

Structurei

3D structure databases

ProteinModelPortaliQ3M672.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 452Alpha-ketoisovalerate bindingUniRule annotation

Sequence similaritiesi

Belongs to the PanB family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CCG. Bacteria.
COG0413. LUCA.
HOGENOMiHOG000078427.
KOiK00606.
OMAiDMLGFFD.
OrthoDBiEOG63C0WN.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
HAMAPiMF_00156. PanB.
InterProiIPR003700. Pantoate_hydroxy_MeTrfase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR20881. PTHR20881. 1 hit.
PfamiPF02548. Pantoate_transf. 1 hit.
[Graphical view]
PIRSFiPIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR00222. panB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q3M672-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVTTQQLIQ WKQQGRSIVA LTAWDYTIAQ ILDAAGVDLI LVGDSMAVML
60 70 80 90 100
GYKTTLPITL EEMLHHAKAV CRGVQRALVV VDLPFLTYQE SIPQAINSAG
110 120 130 140 150
RILKETGAQA VKLEGGYPAM VETITRLVQA GIPVMGHVGL TPQSVHQLGL
160 170 180 190 200
RQQGKTQETA QRILNEAIAL EQAGVFSIVL EHIPADLAMQ ITQKLSIPTI
210 220 230 240 250
GIGAGSHCDG QVLVTSDVLG LSERQPPFAK VYTNLRATIT KAVQDYAAEV

RDRQFPE
Length:257
Mass (Da):27,840
Last modified:October 25, 2005 - v1
Checksum:i5062530B8A567762
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000117 Genomic DNA. Translation: ABA23514.1.

Genome annotation databases

EnsemblBacteriaiABA23514; ABA23514; Ava_3909.
KEGGiava:Ava_3909.
PATRICi35429063. VBIAnaVar43351_5062.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000117 Genomic DNA. Translation: ABA23514.1.

3D structure databases

ProteinModelPortaliQ3M672.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi240292.Ava_3909.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA23514; ABA23514; Ava_3909.
KEGGiava:Ava_3909.
PATRICi35429063. VBIAnaVar43351_5062.

Phylogenomic databases

eggNOGiENOG4105CCG. Bacteria.
COG0413. LUCA.
HOGENOMiHOG000078427.
KOiK00606.
OMAiDMLGFFD.
OrthoDBiEOG63C0WN.

Enzyme and pathway databases

UniPathwayiUPA00028; UER00003.
BioCyciAVAR240292:GCY3-3957-MONOMER.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
HAMAPiMF_00156. PanB.
InterProiIPR003700. Pantoate_hydroxy_MeTrfase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PANTHERiPTHR20881. PTHR20881. 1 hit.
PfamiPF02548. Pantoate_transf. 1 hit.
[Graphical view]
PIRSFiPIRSF000388. Pantoate_hydroxy_MeTrfase. 1 hit.
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR00222. panB. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of Anabaena variabilis ATCC 29413."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29413 / PCC 7937.

Entry informationi

Entry nameiPANB_ANAVT
AccessioniPrimary (citable) accession number: Q3M672
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: October 25, 2005
Last modified: December 9, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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.