ASNO_STRCO
ID ASNO_STRCO Reviewed; 333 AA.
AC Q9Z4Z5;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=L-asparagine oxygenase;
DE EC=1.14.11.39;
DE AltName: Full=L-asparagine 3-hydroxylase;
GN Name=asnO; OrderedLocusNames=SCO3236; ORFNames=SCE29.05c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP ROLE IN CDA BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=A3(2) / 2377, and A3(2) / MT1110;
RX PubMed=17322197; DOI=10.1099/mic.0.2006/002725-0;
RA Neary J.M., Powell A., Gordon L., Milne C., Flett F., Wilkinson B.,
RA Smith C.P., Micklefield J.;
RT "An asparagine oxygenase (AsnO) and a 3-hydroxyasparaginyl
RT phosphotransferase (HasP) are involved in the biosynthesis of calcium-
RT dependent lipopeptide antibiotics.";
RL Microbiology 153:768-776(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP IRON AND PRODUCTS, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP COFACTOR, KINETIC PARAMETERS, STEREOSELECTIVITY, AND REACTION MECHANISM.
RC STRAIN=A3(2) / DSM 40783 / JCM 4979 / NBRC 15732;
RX PubMed=17373765; DOI=10.1021/cb700012y;
RA Strieker M., Kopp F., Mahlert C., Essen L.-O., Marahiel M.A.;
RT "Mechanistic and structural basis of stereospecific Cbeta-hydroxylation in
RT calcium-dependent antibiotic, a daptomycin-type lipopeptide.";
RL ACS Chem. Biol. 2:187-196(2007).
CC -!- FUNCTION: Catalyzes the 3-hydroxylation of L-asparagine to (2S,3S)-3-
CC hydroxyasparagine. The 3-hydroxylated asparagine produced is
CC incorporated at position 9 during the biosynthesis of the non-
CC ribosomally synthesized calcium-dependent antibiotic (CDA), a 11-
CC residue acidic lipopeptide lactone. Is able to hydroxylate only free L-
CC asparagine, since it hydroxylates neither a CDA analog with unmodified
CC Asn at position 9 nor a peptidyl-carrier-protein (PCP)-bound
CC asparagine. Is not active toward D-asparagine.
CC {ECO:0000269|PubMed:17322197, ECO:0000269|PubMed:17373765}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-asparagine + O2 = (2S,3S)-3-
CC hydroxyasparagine + CO2 + succinate; Xref=Rhea:RHEA:25772,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:58048, ChEBI:CHEBI:58850;
CC EC=1.14.11.39; Evidence={ECO:0000269|PubMed:17373765};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:17373765};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:17373765};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=479 uM for L-asparagine {ECO:0000269|PubMed:17373765};
CC -!- PATHWAY: Antibiotic biosynthesis; calcium-dependent antibiotic
CC biosynthesis.
CC -!- DISRUPTION PHENOTYPE: S.coelicolor strain A3(2) / MT1110 and A3(2) /
CC 2377 lacking asnO produce non-hydroxylated asparagine-containing CDA
CC variants, which are not synthesized by the wild-types but retain
CC calcium-dependent antimicrobial activity.
CC {ECO:0000269|PubMed:17322197}.
CC -!- SIMILARITY: Belongs to the clavaminate synthase family. {ECO:0000305}.
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DR EMBL; AL939115; CAB38880.1; -; Genomic_DNA.
DR PIR; T36184; T36184.
DR RefSeq; NP_627448.1; NC_003888.3.
DR RefSeq; WP_003975576.1; NZ_VNID01000025.1.
DR PDB; 2OG5; X-ray; 1.45 A; A=2-333.
DR PDB; 2OG6; X-ray; 1.92 A; A=2-333.
DR PDB; 2OG7; X-ray; 1.66 A; A=2-333.
DR PDBsum; 2OG5; -.
DR PDBsum; 2OG6; -.
DR PDBsum; 2OG7; -.
DR AlphaFoldDB; Q9Z4Z5; -.
DR SMR; Q9Z4Z5; -.
DR STRING; 100226.SCO3236; -.
DR GeneID; 1098670; -.
DR KEGG; sco:SCO3236; -.
DR PATRIC; fig|100226.15.peg.3300; -.
DR eggNOG; COG2175; Bacteria.
DR HOGENOM; CLU_044078_0_0_11; -.
DR InParanoid; Q9Z4Z5; -.
DR OMA; ELTFHTE; -.
DR PhylomeDB; Q9Z4Z5; -.
DR BRENDA; 1.14.11.39; 5998.
DR SABIO-RK; Q9Z4Z5; -.
DR UniPathway; UPA00979; -.
DR EvolutionaryTrace; Q9Z4Z5; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR014503; Clavaminate_syn-like.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 2.
DR PIRSF; PIRSF019543; Clavaminate_syn; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..333
FT /note="L-asparagine oxygenase"
FT /id="PRO_0000350724"
FT BINDING 125
FT /ligand="L-asparagine"
FT /ligand_id="ChEBI:CHEBI:58048"
FT /evidence="ECO:0000269|PubMed:17373765"
FT BINDING 146
FT /ligand="L-asparagine"
FT /ligand_id="ChEBI:CHEBI:58048"
FT /evidence="ECO:0000269|PubMed:17373765"
FT BINDING 155
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:17373765"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:17373765"
FT BINDING 157
FT /ligand="L-asparagine"
FT /ligand_id="ChEBI:CHEBI:58048"
FT /evidence="ECO:0000269|PubMed:17373765"
FT BINDING 158
FT /ligand="L-asparagine"
FT /ligand_id="ChEBI:CHEBI:58048"
FT /evidence="ECO:0000269|PubMed:17373765"
FT BINDING 287
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:17373765"
FT BINDING 301
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:17373765"
FT BINDING 305
FT /ligand="L-asparagine"
FT /ligand_id="ChEBI:CHEBI:58048"
FT /evidence="ECO:0000269|PubMed:17373765"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2OG5"
FT HELIX 18..34
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2OG5"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:2OG5"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:2OG5"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:2OG5"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:2OG5"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:2OG5"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:2OG5"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:2OG5"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:2OG5"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:2OG5"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:2OG7"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:2OG5"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:2OG5"
FT HELIX 250..266
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:2OG5"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 302..310
FT /evidence="ECO:0007829|PDB:2OG5"
FT HELIX 312..318
FT /evidence="ECO:0007829|PDB:2OG5"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:2OG5"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:2OG5"
SQ SEQUENCE 333 AA; 35982 MW; DE394AC07B765580 CRC64;
MAANAAGPAS RYDVTLDQSD AELVEEIAWK LATQATGRPD DAEWVEAARN AWHAWPATLR
RDLAGFRRDS GPDGAIVLRG LPVDSMGLPP TPRVNGSVQR EASLGAAVLL MTACGLGDPG
AFLPEKNGAL VQDVVPVPGM EEFQGNAGST LLTFHNENAF HEHRPDFVML LCLRADPTGR
AGLRTACVRR VLPLLSDSTV DALWAPEFRT APPPSFQLSG PEEAPAPVLL GDRSDPDLRV
DLAATEPVTE RAAEALRELQ AHFDATAVTH RLLPGELAIV DNRVTVHGRT EFTPRYDGTD
RWLQRTFVLT DLRRSRAMRP ADGYVLGAAP QPA
