ID   RFS_RHIO9               Reviewed;         634 AA.
AC   I1C129;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=NRPS-independent siderophore synthetase rfs {ECO:0000303|PubMed:28610916};
DE            Short=NIS rfs {ECO:0000303|PubMed:28610916};
DE            EC=6.-.-.- {ECO:0000269|PubMed:28610916};
DE   AltName: Full=Rhizoferrin biosynthesis protein rfs {ECO:0000303|PubMed:28610916};
GN   Name=rfs {ECO:0000303|PubMed:28610916}; ORFNames=RO3G_06864;
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880;
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(2009).
RN   [2]
RP   FUNCTION, INDUCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-354;
RP   HIS-484 AND LEU-544.
RX   PubMed=28610916; DOI=10.1016/j.biocel.2017.06.005;
RA   Carroll C.S., Grieve C.L., Murugathasan I., Bennet A.J., Czekster C.M.,
RA   Liu H., Naismith J., Moore M.M.;
RT   "The rhizoferrin biosynthetic gene in the fungal pathogen Rhizopus delemar
RT   is a novel member of the NIS gene family.";
RL   Int. J. Biochem. Cell Biol. 89:136-146(2017).
CC   -!- FUNCTION: NRPS-independent siderophore synthetase that catalyzes the
CC       rhizoferrin biosynthesis from citrate and diaminobutane via an ATP-
CC       dependent condensation of citrate with diaminobutane followed by the
CC       addition of a second citrate to the monocitryl-diaminobutane
CC       intermediate (PubMed:28610916). Can also use as substrates the citrate
CC       and diaminobutane homologs oxaloacetic acid, diaminopropane,
CC       diaminobutane, diaminopentane, tricarballylic acid, hydroxylamine and
CC       ornithine (PubMed:28610916). Forms only a mono-substituted intermediate
CC       with oxaloacetic acid and diaminopentane whereas both mono-citryl
CC       intermediates and full rhizoferrin derivatives were detected when
CC       diaminopropane, and ornithine were used as substrates
CC       (PubMed:28610916). Tricarballylic acid only forms a rhizoferrin
CC       derivative, but no mono-substituted intermediate (PubMed:28610916).
CC       {ECO:0000269|PubMed:28610916}.
CC   -!- INDUCTION: Expression is repressed in iron-replete media
CC       (PubMed:28610916). {ECO:0000269|PubMed:28610916}.
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DR   EMBL; CH476736; EIE82159.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1C129; -.
DR   SMR; I1C129; -.
DR   STRING; 936053.I1C129; -.
DR   EnsemblFungi; EIE82159; EIE82159; RO3G_06864.
DR   VEuPathDB; FungiDB:RO3G_06864; -.
DR   eggNOG; ENOG502RX6M; Eukaryota.
DR   InParanoid; I1C129; -.
DR   OMA; THPMHKT; -.
DR   OrthoDB; 1194360at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProt.
DR   GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR   InterPro; IPR007310; Aerobactin_biosyn_IucA/IucC_N.
DR   InterPro; IPR022770; FhuF_domain.
DR   InterPro; IPR037455; LucA/IucC-like.
DR   PANTHER; PTHR34384; PTHR34384; 1.
DR   Pfam; PF06276; FhuF; 1.
DR   Pfam; PF04183; IucA_IucC; 1.
PE   1: Evidence at protein level;
KW   Ligase; Reference proteome.
FT   CHAIN           1..634
FT                   /note="NRPS-independent siderophore synthetase rfs"
FT                   /id="PRO_0000444443"
FT   MUTAGEN         354
FT                   /note="R->A: Does not affect the catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:28610916"
FT   MUTAGEN         484
FT                   /note="H->A: Impairs the catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:28610916"
FT   MUTAGEN         544
FT                   /note="L->R: Enables to accommodate serine in place of
FT                   diaminobutane in the active site and significantly
FT                   increases the catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:28610916"
SQ   SEQUENCE   634 AA;  71816 MW;  C44F7F93F9B9B8C4 CRC64;
     MPVASSEYQN EHYASFATTS RLVTCLVSET LVPVFFVPVK SVDRNNQFIG LCLLLRPTTV
     KQESELPTNI TASDILTVVP LRGLPILNNE RVALFNGIRC PQIDLVDFLD MLPHIYSVES
     SGSLKSGDSL KQKTFDTLSA ILDGNKTFDL VDGYSAVQLW NHFAQDLEIN SKLREQIGQE
     LGSSILFQKY TYDNPKPLPT LNSSTIKWEQ SVVEGHATHP MHKARKSFPP MPPLNPGSYD
     LDHPAVRLVG IPRENAILRG EYEELSAPLV NALMDAGGNH KDIRAQYQNY VFIAIHELQL
     PNIQEKFKDA VIFSKEHQLN VEALASLRSV ARPDILPGLS VKLCLGIKIS SALRTVTPFT
     TYFGPGFSFN VVPKLTYDHE VLAIERELGT ITYRHEDSDV AKHCSSVIRE ALEYDPKYQD
     DLFIPCGALV EKIQRPDTDE TLVAHVWNLD TKEKRVEFLD RYVDFALRSF LPPCLINGVA
     FEAHGQNTLA RFDRKTGLLK GFVIRDFGGV KAHNETLKKS AGVELDILPD SCVEAHSLEE
     VFKLLYHTLF HCQLQRLIRV LDLHYSGEGW EIVRKYLTQY VPKDHVMWPM FMESSKVPGK
     CLVRMKIDEL YRDYIYRPVP NMIKYEPQSV PEAI