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Cytochrome P450 (StaH)

 Q8KLL9_STRTO            Unreviewed;       398 AA.
Q8KLL9;
01-OCT-2002, integrated into UniProtKB/TrEMBL.
01-OCT-2002, sequence version 1.
16-JAN-2019, entry version 76.
SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:KES08710.1};
SubName: Full=StaH {ECO:0000313|EMBL:AAM80533.1};
ORFNames=BU52_01285 {ECO:0000313|EMBL:KES08710.1};
Streptomyces toyocaensis.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=55952 {ECO:0000313|EMBL:AAM80533.1};
[1] {ECO:0000313|EMBL:AAM80533.1}
NUCLEOTIDE SEQUENCE.
STRAIN=NRRL 15009 {ECO:0000313|EMBL:AAM80533.1};
PubMed=9177243; DOI=10.1073/pnas.94.12.6480;
Marshall C.G., Broadhead G., Leskiw B.K., Wright G.D.;
"D-Ala-D-Ala ligases from glycopeptide antibiotic-producing organisms
are highly homologous to the enterococcal vancomycin-resistance
ligases VanA and VanB.";
Proc. Natl. Acad. Sci. U.S.A. 94:6480-6483(1997).
[2] {ECO:0000313|EMBL:AAM80533.1}
NUCLEOTIDE SEQUENCE.
STRAIN=NRRL 15009 {ECO:0000313|EMBL:AAM80533.1};
PubMed=12060705; DOI=10.1073/pnas.102285099;
Pootoolal J., Thomas M.G., Marshall C.G., Neu J.M., Hubbard B.K.,
Walsh C.T., Wright G.D.;
"Assembling the glycopeptide antibiotic scaffold: the biosynthesis of
A47934 from Streptomyces toyocaensis NRRL15009.";
Proc. Natl. Acad. Sci. U.S.A. 99:8962-8967(2002).
[3] {ECO:0000313|EMBL:KES08710.1, ECO:0000313|Proteomes:UP000028341}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NRRL 15009 {ECO:0000313|EMBL:KES08710.1,
ECO:0000313|Proteomes:UP000028341};
Hong H.-J., Kwun M.J.;
"The genome announcement of Streptomyces toyocaensis NRRL15009.";
Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000213|PDB:5EX6}
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH HEME.
PubMed=27477788; DOI=10.1039/c6mb00373g;
Ulrich V., Peschke M., Brieke C., Cryle M.J.;
"More than just recruitment: the X-domain influences catalysis of the
first phenolic coupling reaction in A47934 biosynthesis by Cytochrome
P450 StaH.";
Mol. Biosyst. 12:2992-3004(2016).
-!- SIMILARITY: Belongs to the cytochrome P450 family.
{ECO:0000256|RuleBase:RU000461, ECO:0000256|SAAS:SAAS00578603}.
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EMBL; U82965; AAM80533.1; -; Genomic_DNA.
EMBL; JFCB01000001; KES08710.1; -; Genomic_DNA.
RefSeq; WP_037926416.1; NZ_JFCB01000001.1.
PDB; 5EX6; X-ray; 2.40 A; A/B/C=1-398.
PDBsum; 5EX6; -.
SMR; Q8KLL9; -.
EnsemblBacteria; KES08710; KES08710; BU52_01285.
Proteomes; UP000028341; Unassembled WGS sequence.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR002397; Cyt_P450_B.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00359; BP450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
3D-structure {ECO:0000213|PDB:5EX6};
Complete proteome {ECO:0000313|Proteomes:UP000028341};
Heme {ECO:0000213|PDB:5EX6, ECO:0000256|RuleBase:RU000461,
ECO:0000256|SAAS:SAAS00532861};
Iron {ECO:0000213|PDB:5EX6, ECO:0000256|RuleBase:RU000461,
ECO:0000256|SAAS:SAAS00532861};
Metal-binding {ECO:0000213|PDB:5EX6, ECO:0000256|RuleBase:RU000461,
ECO:0000256|SAAS:SAAS00532861};
Monooxygenase {ECO:0000256|RuleBase:RU000461,
ECO:0000256|SAAS:SAAS00532857};
Oxidoreductase {ECO:0000256|RuleBase:RU000461,
ECO:0000256|SAAS:SAAS00532857};
Reference proteome {ECO:0000313|Proteomes:UP000028341}.
METAL 347 347 Iron (heme axial ligand).
{ECO:0000213|PDB:5EX6}.
SEQUENCE 398 AA; 44073 MW; F5AB70C034490D50 CRC64;
MSGDDRPPIH TLRQGFDPAD ELRAAGELTR VRLGSGADAE HTWLATGHDV VRQVLGDHTR
FSTRRRFDRN DEIGGKGVFR PRELVGNLMD YDPPEHTRLR RLLAPGFTHR KIRRMAPYIE
QIVTERLDEM EREGSPADLI ELFADEVPGP VLCELLGVPR DDRAMFLQLC HRHLDASLSG
RRRAAAGEAF SRYLVTMVAR ERKDPGDGLI GMVVAEHGDT VTDEELRGVC VQMMLAGDDN
ISGMIGLGVL ALLRNPEQIA ALRGDVPAAE RAVDELIRYL TVPYAPTPRT AIEDSTVGDQ
VIKAGETVLC SLPTANRDPA LLPDADRLDV TREAVPHVAF GHGVHHCLGA ALARLELRIA
YTALWRRFPD LRLADPDGAT EFRLSTPAYG ISRLMVTW


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Pathways :
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WP1194: cytochrome P450
WP1219: cytochrome P450
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WP677: Momilactone biosynthesis
WP696: Benzo(a)pyrene metabolism
WP958: cytochrome P450
WP1021: Phase I, non P450
WP1140: Phase I, non P450
WP1213: Phase I, non P450
WP1255: Phase I, non P450
WP1291: Phase I, non P450
WP136: Phase I, non P450
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Related Genes :
[cyp102A1 cyp102 BG04_163] Bifunctional cytochrome P450/NADPH--P450 reductase (Cytochrome P450(BM-3)) (Cytochrome P450BM-3) (Fatty acid monooxygenase) (Flavocytochrome P450 BM3) [Includes: Cytochrome P450 102A1 (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)]
[CYP2C8] Cytochrome P450 2C8 (EC 1.14.14.1) (CYPIIC8) (Cytochrome P450 IIC2) (Cytochrome P450 MP-12) (Cytochrome P450 MP-20) (Cytochrome P450 form 1) (S-mephenytoin 4-hydroxylase)
[CYP2C9 CYP2C10] Cytochrome P450 2C9 (EC 1.14.14.-) ((R)-limonene 6-monooxygenase) (EC 1.14.14.53) ((S)-limonene 6-monooxygenase) (EC 1.14.14.51) ((S)-limonene 7-monooxygenase) (EC 1.14.14.52) (CYPIIC9) (Cholesterol 25-hydroxylase) (EC 1.14.14.-) (Cytochrome P-450MP) (Cytochrome P450 MP-4) (Cytochrome P450 MP-8) (Cytochrome P450 PB-1) (S-mephenytoin 4-hydroxylase)
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[Cyp2d4 Cyp2d-18 Cyp2d-4 Cyp2d18] Cytochrome P450 2D4 (EC 1.14.14.1) (CYPIID18) (CYPIID4) (Cytochrome P450 2D-29) (Cytochrome P450 2D-35) (Cytochrome P450 2D18) (Cytochrome P450-CMF3) (Cytochrome P450-DB4) (Debrisoquine 4-hydroxylase)
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[cypD cyp102A2 yetO yfnJ BSU07250] Bifunctional cytochrome P450/NADPH--P450 reductase 1 (CYP102A2) (Fatty acid hydroxylase CypD) (Flavocytochrome P450 102A2) [Includes: Cytochrome P450 102A2 (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)]
[CYP505] Bifunctional cytochrome P450/NADPH--P450 reductase (Cytochrome P450foxy) (Fatty acid omega-hydroxylase) (P450foxy) [Includes: Cytochrome P450 505 (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)]
[Cyp2b1 Cyp2b-1] Cytochrome P450 2B1 (EC 1.14.14.1) (CYPIIB1) (Cytochrome P450-B) (Cytochrome P450b) (Cytochrome P450-LM2) (Cytochrome P450-PB1) (Cytochrome P450-PB2)
[CYP26B1 CYP26A2 P450RAI2] Cytochrome P450 26B1 (EC 1.14.13.-) (Cytochrome P450 26A2) (Cytochrome P450 retinoic acid-inactivating 2) (Cytochrome P450RAI-2) (Retinoic acid-metabolizing cytochrome)
[CYP21A2 CYP21 CYP21B] Steroid 21-hydroxylase (EC 1.14.14.16) (21-OHase) (Cytochrome P-450c21) (Cytochrome P450 21) (Cytochrome P450 XXI) (Cytochrome P450-C21) (Cytochrome P450-C21B)
[Cyp2b10 Cyp2b-10 Cyp2b20] Cytochrome P450 2B10 (EC 1.14.14.1) (CYPIIB10) (CYPIIB20) (Cytochrome P450 2B20) (Cytochrome P450 clone PF3/46) (Cytochrome P450-16-alpha) (P24) (Testosterone 16-alpha hydroxylase)
[CYP2A6 CYP2A3] Cytochrome P450 2A6 (EC 1.14.13.-) (1,4-cineole 2-exo-monooxygenase) (CYPIIA6) (Coumarin 7-hydroxylase) (Cytochrome P450 IIA3) (Cytochrome P450(I))
[Cyp2c11 Cyp2c Cyp2c-11] Cytochrome P450 2C11 (EC 1.14.14.1) (CYPIIC11) (Cytochrome P-450(M-1)) (Cytochrome P450-UT-2) (Cytochrome P450-UT-A) (Cytochrome P450H)
[Cyp1a1 Cyp1a-1] Cytochrome P450 1A1 (CYP1A1) (EC 1.14.14.1) (CYPIA1) (Cytochrome P450-C) (Cytochrome P450MT2) [Cleaved into: Cytochrome P450MT2A; Cytochrome P450MT2B]
[CYP26A1 CYP26 P450RAI1] Cytochrome P450 26A1 (EC 1.14.13.-) (Cytochrome P450 retinoic acid-inactivating 1) (Cytochrome P450RAI) (hP450RAI) (Retinoic acid 4-hydroxylase) (Retinoic acid-metabolizing cytochrome)
[CYP1A2] Cytochrome P450 1A2 (EC 1.14.14.1) (CYPIA2) (Cholesterol 25-hydroxylase) (Cytochrome P(3)450) (Cytochrome P450 4) (Cytochrome P450-P3)
[Cyp2c13 Cyp2c-13] Cytochrome P450 2C13, male-specific (EC 1.14.14.1) (CYPIIC13) (Cytochrome P-450g) (Cytochrome P450-G) (Cytochrome P450-UT-5)
[Cyp2b2 Cyp2b-2] Cytochrome P450 2B2 (EC 1.14.14.1) (CYPIIB2) (Cytochrome P450 PB4) (Cytochrome P450E)
[CYP55A1 CYP55] NADP nitrous oxide-forming nitric oxide reductase (NOR) (EC 1.7.1.14) (CYPLVA1) (Cytochrome P450 55A1) (Cytochrome P450 DNIR) (Cytochrome P450nor) (Fungal nitric oxide reductase)
[Cyp2d1 Cyp2d-1 Cyp2d9] Cytochrome P450 2D1 (EC 1.14.14.1) (CYPIID1) (Cytochrome P450-CMF1A) (Cytochrome P450-DB1) (Cytochrome P450-UT-7) (Debrisoquine 4-hydroxylase)
[Cyp26b1] Cytochrome P450 26B1 (EC 1.14.13.-) (Cytochrome P450 retinoic acid-inactivating 2) (Cytochrome P450RAI-2)
[Cyp1a2 Cyp1a-2] Cytochrome P450 1A2 (EC 1.14.14.1) (CYPIA2) (Cholesterol 25-hydroxylase) (Cytochrome P-448) (Cytochrome P-450d) (Cytochrome P450-D)
[CYP2C19] Cytochrome P450 2C19 (EC 1.14.14.-) ((R)-limonene 6-monooxygenase) (EC 1.14.14.53) ((S)-limonene 6-monooxygenase) (EC 1.14.14.51) ((S)-limonene 7-monooxygenase) (EC 1.14.14.52) (CYPIIC17) (CYPIIC19) (Cytochrome P450-11A) (Cytochrome P450-254C) (Fenbendazole monooxygenase (4'-hydroxylating)) (EC 1.14.14.75) (Mephenytoin 4-hydroxylase)
[Cyp2e1 Cyp2e Cyp2e-1] Cytochrome P450 2E1 (EC 1.14.13.-) (4-nitrophenol 2-hydroxylase) (EC 1.14.13.n7) (CYPIIE1) (Cytochrome P450-J) (Cytochrome P450RLM6)
[Cyp1b1 Cyp1-b1] Cytochrome P450 1B1 (EC 1.14.14.1) (CYPIB1) (Cytochrome P450CMEF) (Cytochrome P450EF)
[CYP2B6] Cytochrome P450 2B6 (EC 1.14.13.-) (1,4-cineole 2-exo-monooxygenase) (CYPIIB6) (Cytochrome P450 IIB1)
[CYP17A1 CYP17 S17AH] Steroid 17-alpha-hydroxylase/17,20 lyase (EC 1.14.14.19) (17-alpha-hydroxyprogesterone aldolase) (EC 1.14.14.32) (CYPXVII) (Cytochrome P450 17A1) (Cytochrome P450-C17) (Cytochrome P450c17) (Steroid 17-alpha-monooxygenase)
[Cyp1a2 Cyp1a-2] Cytochrome P450 1A2 (EC 1.14.14.1) (CYPIA2) (Cholesterol 25-hydroxylase) (Cytochrome P450-P2) (Cytochrome P450-P3)
[Cyp2d10 Cyp2d-10 Cyp2d5] Cytochrome P450 2D10 (EC 1.14.14.1) (CYPIID10) (Cytochrome P450-CMF1B) (Cytochrome P450-DB5) (Debrisoquine 4-hydroxylase)

Bibliography :
[28144358] Biochemical and structural characterisation of the second oxidative crosslinking step during the biosynthesis of the glycopeptide antibiotic A47934.
[27477788] More than just recruitment: the X-domain influences catalysis of the first phenolic coupling reaction in A47934 biosynthesis by Cytochrome P450 StaH.