ALNC_EMENI
ID ALNC_EMENI Reviewed; 452 AA.
AC C8VJR5;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=NADH-cytochrome b5 reductase-like protein alnC {ECO:0000303|PubMed:30339758};
DE EC=1.6.2.- {ECO:0000305|PubMed:30339758};
DE AltName: Full=Asperlin biosynthesis cluster protein C {ECO:0000303|PubMed:30339758};
GN Name=alnC {ECO:0000303|PubMed:30339758}; ORFNames=ANIA_11198;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=30339758; DOI=10.1021/acschembio.8b00679;
RA Grau M.F., Entwistle R., Chiang Y.M., Ahuja M., Oakley C.E., Akashi T.,
RA Wang C.C.C., Todd R.B., Oakley B.R.;
RT "Hybrid transcription factor engineering activates the silent secondary
RT metabolite gene cluster for (+)-asperlin in Aspergillus nidulans.";
RL ACS Chem. Biol. 13:3193-3205(2018).
CC -!- FUNCTION: NADH-cytochrome b5 reductase-like protein; part of the gene
CC cluster that mediates the biosynthesis of asperlin, a polyketide
CC showing anti-inflammatory, antitumor and antibiotic activities
CC (PubMed:30339758). The first step of the asperlin biosynthesis is the
CC production of the intermediate 2,4,6-octatrienoic acid by the highly
CC redusing polyketide synthase alnA with cleavage of the PKS product by
CC the esterase alnB (PubMed:30339758). 2,4,6-octatrienoic acid is further
CC converted to asperlin via several steps involving the remaining enzymes
CC from the cluster (PubMed:30339758). {ECO:0000269|PubMed:30339758}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P38038};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P38038};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:P38038};
CC Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:P38038};
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:30339758}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is controlled by the asperlin biosynthesis
CC cluster-specific transcription factor alnR.
CC {ECO:0000269|PubMed:30339758}.
CC -!- DISRUPTION PHENOTYPE: Fully eliminates the production of asperlin.
CC {ECO:0000269|PubMed:30339758}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000305}.
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DR EMBL; BN001306; CBF82301.1; -; Genomic_DNA.
DR AlphaFoldDB; C8VJR5; -.
DR SMR; C8VJR5; -.
DR STRING; 162425.CADANIAP00009376; -.
DR EnsemblFungi; CBF82301; CBF82301; ANIA_11198.
DR VEuPathDB; FungiDB:AN11198; -.
DR eggNOG; KOG0534; Eukaryota.
DR eggNOG; KOG0537; Eukaryota.
DR HOGENOM; CLU_003827_0_1_1; -.
DR InParanoid; C8VJR5; -.
DR OrthoDB; 1311668at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.120.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; PTHR19370; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; FMN; Heme; Iron; Membrane; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..452
FT /note="NADH-cytochrome b5 reductase-like protein alnC"
FT /id="PRO_0000445941"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 4..80
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 225..324
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 33..38
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P38038"
FT BINDING 39
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 63
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 80..83
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P38038"
FT BINDING 116..125
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P38038"
FT BINDING 302..305
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P38038"
FT BINDING 389..390
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P38038"
FT BINDING 395..399
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P38038"
SQ SEQUENCE 452 AA; 49968 MW; EE62B25727CA08DE CRC64;
MASPASITLA EVARHSSPND LWIVIEGNVY DVAEYREDHP GGDEILRQFA GKDATTEFQD
AGHSNDAYVK LKTLLVGSLQ SKTLPENQPE ESSRIVSIAV SDRGKIPTKR QARNGNDTSK
YGQLPSLVLA GGLALLFFTL KQHPWQSIQG YLSQAQVSRV QSSGWVGFLG GFLTATTLNT
AAATFVGLTA KKTLLLRHRE LEEYPRVKQH YLPLPPKKPG ISGENTQQFL TLVDRQCIAP
NVYKVRLQGD GLVIGLGQHL KVLAEIDGRK IQRSYTPVSP VGNSPKVDLI IKVYPKGQLG
NYLLNLPLQS RVEIRGPFGR YSPSPTWKHI ACIAGGTGIA PIYQVMRAWP GEITLLYGNE
TWEDILLREE LEQLVLQSPR RIKVHHVLGQ PKSDWKGLRG WITREMIQDL LPEPSSSTGF
LVCGPDGMVR AIRGHFEAID ANGEEKANVF VF
