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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

  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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501Divalent cation 12 Publications
Metal bindingi52 – 521Divalent cation 12 Publications
Metal bindingi56 – 561Divalent cation 12 Publications
Metal bindingi91 – 911Divalent cation 12 Publications
Metal bindingi162 – 1621Divalent cation 22 Publications
Metal bindingi164 – 1641Divalent cation 22 Publications
Metal bindingi168 – 1681Divalent cation 22 Publications
Metal bindingi202 – 2021Divalent cation 22 Publications
Binding sitei223 – 2231Substrate2 Publications

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.
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi107 – 1071K → A: Significant decrease of isomerase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 235235H2HPP isomerasePRO_0000064801Add
BLAST

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

1
235
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 118Combined sources
Beta strandi16 – 194Combined sources
Beta strandi25 – 317Combined sources
Beta strandi34 – 418Combined sources
Beta strandi45 – 506Combined sources
Beta strandi53 – 6917Combined sources
Beta strandi72 – 776Combined sources
Turni78 – 803Combined sources
Beta strandi82 – 854Combined sources
Beta strandi91 – 955Combined sources
Beta strandi97 – 993Combined sources
Beta strandi101 – 1088Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi127 – 1326Combined sources
Beta strandi137 – 1426Combined sources
Beta strandi145 – 1528Combined sources
Turni154 – 1563Combined sources
Beta strandi157 – 1626Combined sources
Beta strandi165 – 1728Combined sources
Beta strandi177 – 1815Combined sources
Beta strandi184 – 1885Combined sources
Beta strandi193 – 1964Combined sources
Beta strandi202 – 2065Combined sources
Beta strandi208 – 2103Combined sources
Beta strandi212 – 2209Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H7JX-ray1.87A/B1-235[»]
3H7YX-ray2.22A/B1-235[»]
3H9AX-ray2.04A/B1-235[»]
ProteinModelPortaliP39639.
SMRiP39639. Positions 2-225.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39639.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 10666Cupin 1CuratedAdd
BLAST
Regioni151 – 21666Cupin 2CuratedAdd
BLAST

Phylogenomic databases

eggNOGiENOG4106CHD. Bacteria.
ENOG410ZIZ7. LUCA.
HOGENOMiHOG000009192.
KOiK19547.
OMAiGYDMTIE.
OrthoDBiEOG63JR7G.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3H7JX-ray1.87A/B1-235[»]
3H7YX-ray2.22A/B1-235[»]
3H9AX-ray2.04A/B1-235[»]
ProteinModelPortaliP39639.
SMRiP39639. Positions 2-225.
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.
OrthoDBiEOG63JR7G.

Enzyme and pathway databases

UniPathwayiUPA00100.
BioCyciBSUB:BSU37730-MONOMER.

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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Guanine nucleotides guanosine 5'-diphosphate 3'-diphosphate and GTP co-operatively regulate the production of an antibiotic bacilysin in Bacillus subtilis."
    Inaoka T., Takahashi K., Ohnishi-Kameyama M., Yoshida M., Ochi K.
    J. Biol. Chem. 278:2169-2176(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, PATHWAY.
    Strain: 168 / 61884.
  4. "bac genes for recombinant bacilysin and anticapsin production in Bacillus host strains."
    Steinborn G., Hajirezaei M.-R., Hofemeister J.
    Arch. Microbiol. 183:71-79(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BACILYSIN PRODUCTION, GENE NAME.
  5. "Investigation of anticapsin biosynthesis reveals a four-enzyme pathway to tetrahydrotyrosine in Bacillus subtilis."
    Mahlstedt S.A., Walsh C.T.
    Biochemistry 49:912-923(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
  6. "Olefin isomerization regiochemistries during tandem action of BacA and BacB on prephenate in bacilysin biosynthesis."
    Parker J.B., Walsh C.T.
    Biochemistry 51:3241-3251(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
  7. "Stereochemical outcome at four stereogenic centers during conversion of prephenate to tetrahydrotyrosine by BacABGF in the bacilysin pathway."
    Parker J.B., Walsh C.T.
    Biochemistry 51:5622-5632(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PATHWAY.
  8. "Role of Bacillus subtilis BacB in the synthesis of bacilysin."
    Rajavel M., Mitra A., Gopal B.
    J. Biol. Chem. 284:31882-31892(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG; COBALT AND IRON IONS, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-107, COFACTOR, PATHWAY, SUBUNIT.
  9. "Analysis of multiple crystal forms of Bacillus subtilis BacB suggests a role for a metal ion as a nucleant for crystallization."
    Rajavel M., Gopal B.
    Acta Crystallogr. D 66:635-639(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG; COABLT AND IRON IONS, COFACTOR, SUBUNIT.

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: July 6, 2016
This is version 96 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.