BACB_BACAM
ID BACB_BACAM Reviewed; 236 AA.
AC Q8KWT0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=H2HPP isomerase {ECO:0000250|UniProtKB:P39639};
DE EC=5.3.3.19 {ECO:0000250|UniProtKB:P39639};
DE AltName: Full=3-((4R)-4-hydroxycyclohexa-1,5-dien-1-yl)-2-oxopropanoate isomerase {ECO:0000250|UniProtKB:P39639};
DE AltName: Full=Bacilysin biosynthesis protein BacB {ECO:0000250|UniProtKB:P39639};
DE AltName: Full=Bi-cupin protein {ECO:0000250|UniProtKB:P39639};
GN Name=bacB {ECO:0000250|UniProtKB:P39639};
OS Bacillus amyloliquefaciens (Bacillus velezensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=1390;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15841;
RX PubMed=15609023; DOI=10.1007/s00203-004-0743-8;
RA Steinborn G., Hajirezaei M.-R., Hofemeister J.;
RT "bac genes for recombinant bacilysin and anticapsin production in Bacillus
RT host strains.";
RL Arch. Microbiol. 183:71-79(2005).
CC -!- FUNCTION: Part of the bacABCDEF operon responsible for the biosynthesis
CC of the nonribosomally synthesized dipeptide antibiotic bacilysin,
CC composed of L-alanine and L-anticapsin. Bacilysin is an irreversible
CC inactivator of the glutaminase domain of glucosamine synthetase. BacB
CC catalyzes the allylic isomerization of the endocyclic-
CC delta(4),delta(8)-7R-dihydro-hydroxyphenylpyruvate (en-H2HPP) to
CC generate a mixture of 3E,7R- and 3Z, 7R-olefins of the exocyclic-
CC delta(3),delta(5)-dihydro-hydroxyphenylpyruvate (ex-H2HPP).
CC {ECO:0000250|UniProtKB:P39639}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate = 3-
CC [(1E,4R)-4-hydroxycyclohex-2-en-1-ylidene]pyruvate;
CC Xref=Rhea:RHEA:33819, ChEBI:CHEBI:84354, ChEBI:CHEBI:84355;
CC EC=5.3.3.19; Evidence={ECO:0000250|UniProtKB:P39639};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P39639};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:P39639};
CC Note=Binds 2 Fe(2+) or Co(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:P39639};
CC -!- PATHWAY: Antibiotic biosynthesis; bacilysin biosynthesis.
CC {ECO:0000250|UniProtKB:P39639}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P39639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; AF396779; AAM90574.1; -; Genomic_DNA.
DR RefSeq; WP_014471185.1; NZ_VRTX01000001.1.
DR AlphaFoldDB; Q8KWT0; -.
DR SMR; Q8KWT0; -.
DR STRING; 692420.BAMF_3606; -.
DR PATRIC; fig|1390.176.peg.1784; -.
DR eggNOG; COG1917; Bacteria.
DR UniPathway; UPA00100; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050897; F:cobalt ion binding; ISS:UniProtKB.
DR GO; GO:0016863; F:intramolecular oxidoreductase activity, transposing C=C bonds; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; ISS:UniProtKB.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR013096; Cupin_2.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF07883; Cupin_2; 2.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis; Cobalt; Cytoplasm; Iron; Isomerase; Metal-binding.
FT CHAIN 1..236
FT /note="H2HPP isomerase"
FT /id="PRO_0000064800"
FT REGION 40..106
FT /note="Cupin 1"
FT /evidence="ECO:0000305"
FT REGION 151..215
FT /note="Cupin 2"
FT /evidence="ECO:0000305"
FT BINDING 50
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P39639"
FT BINDING 52
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P39639"
FT BINDING 56
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P39639"
FT BINDING 91
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P39639"
FT BINDING 162
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P39639"
FT BINDING 164
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P39639"
FT BINDING 168
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P39639"
FT BINDING 202
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P39639"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P39639"
SQ SEQUENCE 236 AA; 26794 MW; 5BD923ECC41FAE8C CRC64;
MKTKQDLQEL YFPTPKLIEW ENGVRQYSSV RGDTEVLLSY VPPHTNVEPH QHKEVQIGLV
VSGELSMTVG DVTRKMTALE SAYIAPPYVP HGARNETDQE VIAIDIKRLK AGETYTSPED
YFLNIFKTRD LLPGMEVTFF VEDWVEIMLA NIPGNGGEMP FHKHRNEQIG ICIGGGYDMT
IEGCKVDMTF GTAYFCDPRE DHGAINRFEK DSKSVNIFFP PRYNRAKAKK LEAKES
