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Protein

H2HPP isomerase

Gene

bacB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of the bacABCDEF operon responsible for the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase (PubMed:15609023, PubMed:20052993). BacB catalyzes the allylic isomerization of the endocyclic-delta4,delta(8)-7R-dihydro-hydroxyphenylpyruvate (en-H2HPP) to generate a mixture of 3E,7R- and 3Z, 7R-olefins (E/Z ration of 3/1) of the exocyclic-delta3,delta(5)-dihydro-hydroxyphenylpyruvate (ex-H2HPP) (PubMed:20052993, PubMed:22483065, PubMed:22765234, PubMed:19776011).5 Publications

Catalytic activityi

3-((4R)-4-hydroxycyclohexa-1,5-dien-1-yl)-2-oxopropanoate = 3-((1E,4R)-4-hydroxycyclohex-2-en-1-ylidene)-2-oxopropanoate.3 Publications

Cofactori

Fe2+2 Publications, Co2+2 PublicationsNote: Binds 2 Fe2+ or Co2+ ions per subunit.2 Publications

Kineticsi

Kcat is 1471 min(-1) for isomerase activity with en-H2HPP as substrate.1 Publication

Manual assertion based on experiment ini

  1. KM=423 µM for en-H2HPP1 Publication
  1. Vmax=53.49 nmol/min/µg enzyme1 Publication

Pathwayi: bacilysin biosynthesis

This protein is involved in the pathway bacilysin biosynthesis, which is part of Antibiotic biosynthesis.4 Publications1 Publication
View all proteins of this organism that are known to be involved in the pathway bacilysin biosynthesis and in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi50Divalent cation 12 Publications1
Metal bindingi52Divalent cation 12 Publications1
Metal bindingi56Divalent cation 12 Publications1
Metal bindingi91Divalent cation 12 Publications1
Metal bindingi162Divalent cation 22 Publications1
Metal bindingi164Divalent cation 22 Publications1
Metal bindingi168Divalent cation 22 Publications1
Metal bindingi202Divalent cation 22 Publications1
Binding sitei223Substrate2 Publications1

GO - Molecular functioni

  • cobalt ion binding Source: UniProtKB
  • intramolecular oxidoreductase activity, transposing C=C bonds Source: UniProtKB
  • iron ion binding Source: UniProtKB

GO - Biological processi

  • antibiotic biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

Cobalt, Iron, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU37730-MONOMER.
MetaCyc:MONOMER-19124.
UniPathwayiUPA00100.

Names & Taxonomyi

Protein namesi
Recommended name:
H2HPP isomeraseCurated (EC:5.3.3.193 Publications)
Alternative name(s):
3-((4R)-4-hydroxycyclohexa-1,5-dien-1-yl)-2-oxopropanoate isomeraseCurated
Bacilysin biosynthesis protein BacB1 Publication
Bi-cupin protein1 Publication
Gene namesi
Name:bacB1 Publication
Synonyms:ywfC1 Publication
Ordered Locus Names:BSU37730
ORF Names:ipa-81d
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi107K → A: Significant decrease of isomerase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000648011 – 235H2HPP isomeraseAdd BLAST235

Proteomic databases

PaxDbiP39639.

Expressioni

Inductioni

The compound guanosine 5'-diphosphate 3'-diphosphate (ppGpp) is essential for the transcription of the bacABCDEF operon and BacG, and GTP regulates the transcription of both this operon and ywfH via the CodY-mediated regulation system.1 Publication

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100020381.

Structurei

Secondary structure

1235
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 11Combined sources8
Beta strandi16 – 19Combined sources4
Beta strandi25 – 31Combined sources7
Beta strandi34 – 41Combined sources8
Beta strandi45 – 50Combined sources6
Beta strandi53 – 69Combined sources17
Beta strandi72 – 77Combined sources6
Turni78 – 80Combined sources3
Beta strandi82 – 85Combined sources4
Beta strandi91 – 95Combined sources5
Beta strandi97 – 99Combined sources3
Beta strandi101 – 108Combined sources8
Beta strandi121 – 123Combined sources3
Beta strandi127 – 132Combined sources6
Beta strandi137 – 142Combined sources6
Beta strandi145 – 152Combined sources8
Turni154 – 156Combined sources3
Beta strandi157 – 162Combined sources6
Beta strandi165 – 172Combined sources8
Beta strandi177 – 181Combined sources5
Beta strandi184 – 188Combined sources5
Beta strandi193 – 196Combined sources4
Beta strandi202 – 206Combined sources5
Beta strandi208 – 210Combined sources3
Beta strandi212 – 220Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3H7JX-ray1.87A/B1-235[»]
3H7YX-ray2.22A/B1-235[»]
3H9AX-ray2.04A/B1-235[»]
ProteinModelPortaliP39639.
SMRiP39639.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39639.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni41 – 106Cupin 1CuratedAdd BLAST66
Regioni151 – 216Cupin 2CuratedAdd BLAST66

Phylogenomic databases

eggNOGiENOG4106CHD. Bacteria.
ENOG410ZIZ7. LUCA.
HOGENOMiHOG000009192.
KOiK19547.
OMAiGYDMTIE.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR013096. Cupin_2.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF07883. Cupin_2. 2 hits.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.

Sequencei

Sequence statusi: Complete.

P39639-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTKEDMQEL YFPTPKLIEW ENGVRQYSTV RGDTEVLMSY VPPHTNVEPH
60 70 80 90 100
QHKEVQIGMV VSGELMMTVG DVTRKMTALE SAYIAPPHVP HGARNDTDQE
110 120 130 140 150
VIAIDIKRLK ADETYTSPED YFLDIFKTRD LLPGMEVTFF VEDWVEIMLA
160 170 180 190 200
KIPGNGGEMP FHKHRNEQIG ICIGGGYDMT VEGCTVEMKF GTAYFCEPRE
210 220 230
DHGAINRSEK ESKSINIFFP PRYNRAKAKK MKADE
Length:235
Mass (Da):26,840
Last modified:February 1, 1995 - v1
Checksum:i9A9A1608148D0FA6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73124 Genomic DNA. Translation: CAA51637.1.
AL009126 Genomic DNA. Translation: CAB15800.1.
PIRiS39736.
RefSeqiNP_391653.1. NC_000964.3.
WP_003244300.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15800; CAB15800; BSU37730.
GeneIDi937084.
KEGGibsu:BSU37730.
PATRICi18979584. VBIBacSub10457_3954.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73124 Genomic DNA. Translation: CAA51637.1.
AL009126 Genomic DNA. Translation: CAB15800.1.
PIRiS39736.
RefSeqiNP_391653.1. NC_000964.3.
WP_003244300.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3H7JX-ray1.87A/B1-235[»]
3H7YX-ray2.22A/B1-235[»]
3H9AX-ray2.04A/B1-235[»]
ProteinModelPortaliP39639.
SMRiP39639.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100020381.

Proteomic databases

PaxDbiP39639.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15800; CAB15800; BSU37730.
GeneIDi937084.
KEGGibsu:BSU37730.
PATRICi18979584. VBIBacSub10457_3954.

Phylogenomic databases

eggNOGiENOG4106CHD. Bacteria.
ENOG410ZIZ7. LUCA.
HOGENOMiHOG000009192.
KOiK19547.
OMAiGYDMTIE.

Enzyme and pathway databases

UniPathwayiUPA00100.
BioCyciBSUB:BSU37730-MONOMER.
MetaCyc:MONOMER-19124.

Miscellaneous databases

EvolutionaryTraceiP39639.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR013096. Cupin_2.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF07883. Cupin_2. 2 hits.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiBACB_BACSU
AccessioniPrimary (citable) accession number: P39639
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 99 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.