ID   NOVN_STRNV              Reviewed;         677 AA.
AC   Q9L9F4;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 2.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Decarbamoylnovobiocin carbamoyltransferase;
DE            EC=2.1.3.12;
DE   AltName: Full=Novobiocin biosynthesis protein N;
GN   Name=novN;
OS   Streptomyces niveus (Streptomyces spheroides).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=193462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC   2449;
RX   PubMed=10770754; DOI=10.1128/aac.44.5.1214-1222.2000;
RA   Steffensky M., Muhlenweg A., Wang Z.X., Li S.M., Heide L.;
RT   "Identification of the novobiocin biosynthetic gene cluster of Streptomyces
RT   spheroides NCIB 11891.";
RL   Antimicrob. Agents Chemother. 44:1214-1222(2000).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC   STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC   2449;
RX   PubMed=14694473; DOI=10.1002/anie.200352626;
RA   Freel Meyers C.L., Oberthur M., Xu H., Heide L., Kahne D., Walsh C.T.;
RT   "Characterization of NovP and NovN: completion of novobiocin biosynthesis
RT   by sequential tailoring of the noviosyl ring.";
RL   Angew. Chem. Int. Ed. 43:67-70(2004).
RN   [3]
RP   CRYSTALLIZATION.
RX   PubMed=18997325; DOI=10.1107/s1744309108030145;
RA   Gomez Garcia I., Freel Meyers C.L., Walsh C.T., Lawson D.M.;
RT   "Crystallization and preliminary X-ray analysis of the O-
RT   carbamoyltransferase NovN from the novobiocin-biosynthetic cluster of
RT   Streptomyces spheroides.";
RL   Acta Crystallogr. F 64:1000-1002(2008).
CC   -!- FUNCTION: Carbamoyltransferase that mediates 3'-carbamoylation of the
CC       noviosyl ring to produce novobiocin, the final step in the novobiocin
CC       biosynthesis pathway. Novobiocincin is an aminocoumarin family
CC       antibiotic that targets bacterial DNA gyrases.
CC       {ECO:0000269|PubMed:14694473}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + descarbamoylnovobiocin = novobiocin +
CC         phosphate; Xref=Rhea:RHEA:36659, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58228, ChEBI:CHEBI:71339, ChEBI:CHEBI:73955; EC=2.1.3.12;
CC         Evidence={ECO:0000269|PubMed:14694473};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.6 uM for decarbamoylnovobiocin {ECO:0000269|PubMed:14694473};
CC         KM=5.1 uM for carbamoyl phosphate {ECO:0000269|PubMed:14694473};
CC         Note=kcat is 4.1 min(-1) with decarbamoylnovobiocin as substrate.;
CC   -!- PATHWAY: Antibiotic biosynthesis; novobiocin biosynthesis.
CC       {ECO:0000269|PubMed:14694473}.
CC   -!- SIMILARITY: Belongs to the NodU/CmcH family. {ECO:0000305}.
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DR   EMBL; AF170880; AAF67507.2; -; Genomic_DNA.
DR   RefSeq; WP_069626144.1; NZ_MDCR01000039.1.
DR   AlphaFoldDB; Q9L9F4; -.
DR   SMR; Q9L9F4; -.
DR   KEGG; ag:AAF67507; -.
DR   BioCyc; MetaCyc:MON-18052; -.
DR   BRENDA; 2.1.3.12; 6099.
DR   UniPathway; UPA01035; -.
DR   GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0043642; P:novobiocin biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.90.870.20; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR031730; Carbam_trans_C.
DR   InterPro; IPR038152; Carbam_trans_C_sf.
DR   InterPro; IPR003696; Carbtransf_dom.
DR   Pfam; PF16861; Carbam_trans_C; 1.
DR   Pfam; PF02543; Carbam_trans_N; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Transferase.
FT   CHAIN           1..677
FT                   /note="Decarbamoylnovobiocin carbamoyltransferase"
FT                   /id="PRO_0000424001"
SQ   SEQUENCE   677 AA;  74340 MW;  6A2EE607E5948A1C CRC64;
     MLILGLNGNV SAAGADVVPN LNELYMHDAA ATLVRDGVLV AAVEEERLNR IKKTTKFPSN
     AIRECLAAAG AKPADVDAIA YYFPEDFFDD IFQQLYTEHP SVPTRYSREM ILERLRVDLG
     WAAPPDILHY VPHHLAHAMS TYYRSGMREA LVVVMDGAGE RNCTTIYRSD GAELFEIASY
     PVPKSLGMFY LYGTRHLGYG FGDEYKVMGL APYGDPSTYR DVFSTLYSLG PNGTYELIPR
     GGVVFRMTTI LREHGLQPRR RGEPFTQAHM DFAASVQETT EQIAMHVIGY WARSTGLRNL
     AFGGGVAHNS TLNGRILTSG LFDEVFVHPA SHDAGSSEGA ALVVARERGE RVWPLPRLTN
     ASLGPDLGDV DSLERTLKSW SPLVDVERPD DIVEATAHLL AAGEAIGWAH GRSEFGPRAL
     GNRSILADAR PKENQTRINA MVKKRESFRP FAPVVTAEAA GDYFDLPETV GHHDFMSFVV
     QVRADRRELL GAVTHVDGSA RVQVVTEETN PRFHRLVTRF GELTGTPVLL NTSFNNHAEP
     IVQSVDDVLT SYLTTSLDVL VIEDFVVRRR TELPLALEDF TIGFRPVTRL VRRLADVSAG
     RPGAPEVSHE IYLDHTSGPR ATISAAMYEL LTHADGVTPL GSLGIELTGE LLTELYDLWQ
     GRFVTVAPVG DGAGSAP