ID M5BBI5_9MICO Unreviewed; 456 AA.
AC M5BBI5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN ORFNames=CMN_02767 {ECO:0000313|EMBL:CCE76696.1};
OS Clavibacter nebraskensis NCPPB 2581.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Clavibacter.
OX NCBI_TaxID=1097677 {ECO:0000313|EMBL:CCE76696.1};
RN [1] {ECO:0000313|EMBL:CCE76696.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Type strain: NCPPB 2581 {ECO:0000313|EMBL:CCE76696.1};
RA Gartemann K.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCE76696.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Type strain: NCPPB 2581 {ECO:0000313|EMBL:CCE76696.1};
RA Gartemann K.H., Blom J., Dreiseikelmann B., Fluegel M., Jaenicke S.,
RA Linke B., Sczcepanowski R., Wittmann J., Goesmann A., Puehler A.,
RA Eichenlaub R., Rueckert C.;
RT "The genome sequence of the maize-pathogen Clavibacter michiganensis subsp.
RT nebraskensis.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.18.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001005};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000362-1};
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008312}.
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DR EMBL; HE614873; CCE76696.1; -; Genomic_DNA.
DR RefSeq; WP_015491366.1; NC_020891.1.
DR AlphaFoldDB; M5BBI5; -.
DR KEGG; cmc:CMN_02767; -.
DR HOGENOM; CLU_024722_4_0_11; -.
DR Proteomes; UP000012170; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR021163; Ferredox_Rdtase_adrenod.
DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF91; NADPH:ADRENODOXIN OXIDOREDUCTASE, MITOCHONDRIAL; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF000362; FNR; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000362-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR000362-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 5..168
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 151..154
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 195..196
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 207
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 361
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 368..370
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 368
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
SQ SEQUENCE 456 AA; 50426 MW; 731C2256BD2F9016 CRC64;
MTKLRLAIVG AGPAGIYAAD IILKAEKQFD VSIDLFERLP APYGLVRYGV APDHPRIKGI
IGALRDVLDR GDIRIFGNVD YGRDITLEDL QRHYNAVIFS TGAIRDAELD IPGIDLPGSY
GAAEFVNWFD GHPDFPRDWP LDAREVAVIG NGNVALDVAR MLAKHADDLL PTEIPDNVYT
GLKHSPVTDV HVFGRRGPAQ VKFTPLELRE LGEVPDVDVI VYDEDFGVDP AAEEAAKTNK
QVMVISRVLE KWRTRETGSA SRRLHLHFYS RPAEVLASDD AEPRVAGLRI ERTRPDGLGG
VEGTGEYRDF PVQAIYRAVG YFGSPVDGIP FDEVRGVIPN HEGQVLDLDN TRIPGVYATG
WIKRGPIGLI GHTKSDAMET VSHVLNDQGD WWTPEAPEEQ AIVDLLAERG VEYTDLAGWH
ALDEHEIALG RPHGRARIKV VERDEMLKAS RPRESV
//
