CYPX_BACSU
ID CYPX_BACSU Reviewed; 405 AA.
AC O34926;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Pulcherriminic acid synthase;
DE EC=1.14.15.13;
DE AltName: Full=CYP134A1;
DE AltName: Full=Cyclo-L-leucyl-L-leucyl dipeptide oxidase;
DE AltName: Full=Cytochrome P450 CypX;
GN Name=cypX; Synonyms=cyp134, cypB; OrderedLocusNames=BSU35060;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.;
RT "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT subtilis.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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 X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=20690619; DOI=10.1021/bi100910y;
RA Cryle M.J., Bell S.G., Schlichting I.;
RT "Structural and biochemical characterization of the cytochrome P450 CypX
RT (CYP134A1) from Bacillus subtilis: a cyclo-L-leucyl-L-leucyl dipeptide
RT oxidase.";
RL Biochemistry 49:7282-7296(2010).
CC -!- FUNCTION: Involved in the biosynthesis of pulcherrimin, a red
CC extracellular pigment. Catalyzes the oxidation of cyclo(L-Leu-L-Leu)
CC (cLL) to yield pulcherriminic acid which forms pulcherrimin via a
CC nonenzymic reaction with Fe(3+). Substrates with small alkyl groups
CC (cAA, cLG, cLP) exhibit weaker binding to CYP134A1, but substrates with
CC larger hydrophobic side chains bind in a similar regime to cLL.
CC {ECO:0000269|PubMed:20690619}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclo(L-leucyl-L-leucyl) + 4 H(+) + 3 O2 + 6 reduced [2Fe-2S]-
CC [ferredoxin] = 4 H2O + 6 oxidized [2Fe-2S]-[ferredoxin] +
CC pulcherriminic acid; Xref=Rhea:RHEA:35555, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:67269, ChEBI:CHEBI:77663; EC=1.14.15.13;
CC Evidence={ECO:0000269|PubMed:20690619};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:20690619};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20690619}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF017113; AAC67280.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15511.1; -; Genomic_DNA.
DR PIR; F69611; F69611.
DR RefSeq; NP_391386.1; NC_000964.3.
DR RefSeq; WP_003244436.1; NZ_JNCM01000033.1.
DR PDB; 3NC3; X-ray; 2.66 A; A/B=1-405.
DR PDB; 3NC5; X-ray; 2.90 A; A/B=1-405.
DR PDB; 3NC6; X-ray; 3.10 A; A/B=1-405.
DR PDB; 3NC7; X-ray; 3.30 A; A/B=1-405.
DR PDBsum; 3NC3; -.
DR PDBsum; 3NC5; -.
DR PDBsum; 3NC6; -.
DR PDBsum; 3NC7; -.
DR AlphaFoldDB; O34926; -.
DR SMR; O34926; -.
DR STRING; 224308.BSU35060; -.
DR jPOST; O34926; -.
DR PaxDb; O34926; -.
DR PRIDE; O34926; -.
DR EnsemblBacteria; CAB15511; CAB15511; BSU_35060.
DR GeneID; 936624; -.
DR KEGG; bsu:BSU35060; -.
DR PATRIC; fig|224308.179.peg.3795; -.
DR eggNOG; COG2124; Bacteria.
DR InParanoid; O34926; -.
DR OMA; CDFARDV; -.
DR PhylomeDB; O34926; -.
DR BioCyc; BSUB:BSU35060-MON; -.
DR BioCyc; MetaCyc:BSU35060-MON; -.
DR BRENDA; 1.14.15.13; 658.
DR EvolutionaryTrace; O34926; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0036199; F:cholest-4-en-3-one 26-monooxygenase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0016713; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0006707; P:cholesterol catabolic process; IBA:GO_Central.
DR GO; GO:0046148; P:pigment biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR030904; CypX.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR TIGRFAMs; TIGR04538; P450_cycloAA_1; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..405
FT /note="Pulcherriminic acid synthase"
FT /id="PRO_0000052234"
FT BINDING 62
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:20690619"
FT BINDING 229
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:20690619"
FT BINDING 285
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:20690619"
FT BINDING 353
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT HELIX 13..17
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:3NC3"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:3NC3"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:3NC3"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:3NC3"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3NC3"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:3NC7"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3NC6"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 100..116
FT /evidence="ECO:0007829|PDB:3NC3"
FT TURN 117..123
FT /evidence="ECO:0007829|PDB:3NC3"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 151..166
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 172..196
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 220..250
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:3NC3"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:3NC3"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:3NC3"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:3NC5"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 308..312
FT /evidence="ECO:0007829|PDB:3NC3"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:3NC3"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:3NC3"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:3NC3"
FT HELIX 356..373
FT /evidence="ECO:0007829|PDB:3NC3"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:3NC3"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:3NC3"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:3NC3"
SQ SEQUENCE 405 AA; 45473 MW; A943DDFEAB67BD01 CRC64;
MSQSIKLFSV LSDQFQNNPY AYFSQLREED PVHYEESIDS YFISRYHDVR YILQHPDIFT
TKSLVERAEP VMRGPVLAQM HGKEHSAKRR IVVRSFIGDA LDHLSPLIKQ NAENLLAPYL
ERGKSDLVND FGKTFAVCVT MDMLGLDKRD HEKISEWHSG VADFITSISQ SPEARAHSLW
CSEQLSQYLM PVIKERRVNP GSDLISILCT SEYEGMALSD KDILALILNV LLAATEPADK
TLALMIYHLL NNPEQMNDVL ADRSLVPRAI AETLRYKPPV QLIPRQLSQD TVVGGMEIKK
DTIVFCMIGA ANRDPEAFEQ PDVFNIHRED LGIKSAFSGA ARHLAFGSGI HNCVGAAFAK
NEIEIVANIV LDKMRNIRLE EDFCYAESGL YTRGPVSLLV AFDGA
