BACB_BACSU
ID BACB_BACSU Reviewed; 235 AA.
AC P39639;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=H2HPP isomerase {ECO:0000305};
DE EC=5.3.3.19 {ECO:0000269|PubMed:19776011, ECO:0000269|PubMed:20052993, ECO:0000269|PubMed:22483065};
DE AltName: Full=3-((4R)-4-hydroxycyclohexa-1,5-dien-1-yl)-2-oxopropanoate isomerase {ECO:0000305};
DE AltName: Full=Bacilysin biosynthesis protein BacB {ECO:0000303|PubMed:15609023};
DE AltName: Full=Bi-cupin protein {ECO:0000303|PubMed:19776011};
GN Name=bacB {ECO:0000303|PubMed:15609023};
GN Synonyms=ywfC {ECO:0000303|PubMed:20052993}; OrderedLocusNames=BSU37730;
GN ORFNames=ipa-81d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INDUCTION, AND PATHWAY.
RC STRAIN=168 / 61884;
RX PubMed=12372825; DOI=10.1074/jbc.m208722200;
RA Inaoka T., Takahashi K., Ohnishi-Kameyama M., Yoshida M., Ochi K.;
RT "Guanine nucleotides guanosine 5'-diphosphate 3'-diphosphate and GTP co-
RT operatively regulate the production of an antibiotic bacilysin in Bacillus
RT subtilis.";
RL J. Biol. Chem. 278:2169-2176(2003).
RN [4]
RP FUNCTION IN BACILYSIN PRODUCTION, AND GENE NAME.
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).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=20052993; DOI=10.1021/bi9021186;
RA Mahlstedt S.A., Walsh C.T.;
RT "Investigation of anticapsin biosynthesis reveals a four-enzyme pathway to
RT tetrahydrotyrosine in Bacillus subtilis.";
RL Biochemistry 49:912-923(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=22483065; DOI=10.1021/bi300254u;
RA Parker J.B., Walsh C.T.;
RT "Olefin isomerization regiochemistries during tandem action of BacA and
RT BacB on prephenate in bacilysin biosynthesis.";
RL Biochemistry 51:3241-3251(2012).
RN [7]
RP FUNCTION, AND PATHWAY.
RX PubMed=22765234; DOI=10.1021/bi3006362;
RA Parker J.B., Walsh C.T.;
RT "Stereochemical outcome at four stereogenic centers during conversion of
RT prephenate to tetrahydrotyrosine by BacABGF in the bacilysin pathway.";
RL Biochemistry 51:5622-5632(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG;
RP COBALT AND IRON IONS, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, MUTAGENESIS OF LYS-107, COFACTOR, PATHWAY, AND SUBUNIT.
RX PubMed=19776011; DOI=10.1074/jbc.m109.014522;
RA Rajavel M., Mitra A., Gopal B.;
RT "Role of Bacillus subtilis BacB in the synthesis of bacilysin.";
RL J. Biol. Chem. 284:31882-31892(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG;
RP COABLT AND IRON IONS, COFACTOR, AND SUBUNIT.
RX PubMed=20445239; DOI=10.1107/s0907444910006682;
RA Rajavel M., Gopal B.;
RT "Analysis of multiple crystal forms of Bacillus subtilis BacB suggests a
RT role for a metal ion as a nucleant for crystallization.";
RL Acta Crystallogr. D 66:635-639(2010).
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
CC (PubMed:15609023, PubMed:20052993). BacB catalyzes the allylic
CC isomerization of the endocyclic-delta(4),delta(8)-7R-dihydro-
CC hydroxyphenylpyruvate (en-H2HPP) to generate a mixture of 3E,7R- and
CC 3Z, 7R-olefins (E/Z ration of 3/1) of the exocyclic-delta(3),delta(5)-
CC dihydro-hydroxyphenylpyruvate (ex-H2HPP) (PubMed:20052993,
CC PubMed:22483065, PubMed:22765234, PubMed:19776011).
CC {ECO:0000269|PubMed:15609023, ECO:0000269|PubMed:19776011,
CC ECO:0000269|PubMed:20052993, ECO:0000269|PubMed:22483065,
CC ECO:0000269|PubMed:22765234}.
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:0000269|PubMed:19776011,
CC ECO:0000269|PubMed:20052993, ECO:0000269|PubMed:22483065};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:19776011, ECO:0000269|PubMed:20445239};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:19776011, ECO:0000269|PubMed:20445239};
CC Note=Binds 2 Fe(2+) or Co(2+) ions per subunit.
CC {ECO:0000269|PubMed:19776011, ECO:0000269|PubMed:20445239};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=423 uM for en-H2HPP {ECO:0000269|PubMed:19776011};
CC Vmax=53.49 nmol/min/ug enzyme {ECO:0000269|PubMed:19776011};
CC Note=kcat is 1471 min(-1) for isomerase activity with en-H2HPP as
CC substrate. {ECO:0000269|PubMed:19776011};
CC -!- PATHWAY: Antibiotic biosynthesis; bacilysin biosynthesis.
CC {ECO:0000269|PubMed:22765234, ECO:0000305|PubMed:12372825,
CC ECO:0000305|PubMed:19776011, ECO:0000305|PubMed:20052993,
CC ECO:0000305|PubMed:22483065}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19776011,
CC ECO:0000269|PubMed:20445239}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: The compound guanosine 5'-diphosphate 3'-diphosphate (ppGpp)
CC is essential for the transcription of the bacABCDEF operon and BacG,
CC and GTP regulates the transcription of both this operon and ywfH via
CC the CodY-mediated regulation system. {ECO:0000269|PubMed:12372825}.
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DR EMBL; X73124; CAA51637.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15800.1; -; Genomic_DNA.
DR PIR; S39736; S39736.
DR RefSeq; NP_391653.1; NC_000964.3.
DR RefSeq; WP_003244300.1; NZ_JNCM01000034.1.
DR PDB; 3H7J; X-ray; 1.87 A; A/B=1-235.
DR PDB; 3H7Y; X-ray; 2.22 A; A/B=1-235.
DR PDB; 3H9A; X-ray; 2.04 A; A/B=1-235.
DR PDBsum; 3H7J; -.
DR PDBsum; 3H7Y; -.
DR PDBsum; 3H9A; -.
DR AlphaFoldDB; P39639; -.
DR SMR; P39639; -.
DR STRING; 224308.BSU37730; -.
DR DrugBank; DB03884; Phenylpyruvic acid.
DR PaxDb; P39639; -.
DR PRIDE; P39639; -.
DR EnsemblBacteria; CAB15800; CAB15800; BSU_37730.
DR GeneID; 937084; -.
DR KEGG; bsu:BSU37730; -.
DR PATRIC; fig|224308.179.peg.4085; -.
DR eggNOG; COG1917; Bacteria.
DR OMA; GYDMTIE; -.
DR BioCyc; BSUB:BSU37730-MON; -.
DR BioCyc; MetaCyc:MON-19124; -.
DR BRENDA; 5.3.3.19; 658.
DR UniPathway; UPA00100; -.
DR EvolutionaryTrace; P39639; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR GO; GO:0016863; F:intramolecular oxidoreductase activity, transposing C=C bonds; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA: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 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Cobalt; Cytoplasm; Iron; Isomerase;
KW Metal-binding; Reference proteome.
FT CHAIN 1..235
FT /note="H2HPP isomerase"
FT /id="PRO_0000064801"
FT REGION 41..106
FT /note="Cupin 1"
FT /evidence="ECO:0000305"
FT REGION 151..216
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:0000269|PubMed:19776011,
FT ECO:0000269|PubMed:20445239"
FT BINDING 52
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19776011,
FT ECO:0000269|PubMed:20445239"
FT BINDING 56
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19776011,
FT ECO:0000269|PubMed:20445239"
FT BINDING 91
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19776011,
FT ECO:0000269|PubMed:20445239"
FT BINDING 162
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19776011,
FT ECO:0000269|PubMed:20445239"
FT BINDING 164
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19776011,
FT ECO:0000269|PubMed:20445239"
FT BINDING 168
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19776011,
FT ECO:0000269|PubMed:20445239"
FT BINDING 202
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19776011,
FT ECO:0000269|PubMed:20445239"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19776011,
FT ECO:0000269|PubMed:20445239"
FT MUTAGEN 107
FT /note="K->A: Significant decrease of isomerase activity."
FT /evidence="ECO:0000269|PubMed:19776011"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 53..69
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:3H7J"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:3H9A"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:3H7J"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3H7J"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:3H7J"
SQ SEQUENCE 235 AA; 26840 MW; 9A9A1608148D0FA6 CRC64;
MKTKEDMQEL YFPTPKLIEW ENGVRQYSTV RGDTEVLMSY VPPHTNVEPH QHKEVQIGMV
VSGELMMTVG DVTRKMTALE SAYIAPPHVP HGARNDTDQE VIAIDIKRLK ADETYTSPED
YFLDIFKTRD LLPGMEVTFF VEDWVEIMLA KIPGNGGEMP FHKHRNEQIG ICIGGGYDMT
VEGCTVEMKF GTAYFCEPRE DHGAINRSEK ESKSINIFFP PRYNRAKAKK MKADE
