ID A0A1S1NH41_9MYCO Unreviewed; 561 AA.
AC A0A1S1NH41;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN Name=fprB_1 {ECO:0000313|EMBL:PQM49002.1};
GN ORFNames=BKN37_16260 {ECO:0000313|EMBL:OHV02027.1}, C1Y40_00777
GN {ECO:0000313|EMBL:PQM49002.1};
OS Mycobacterium talmoniae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1858794 {ECO:0000313|EMBL:OHV02027.1, ECO:0000313|Proteomes:UP000179734};
RN [1] {ECO:0000313|EMBL:OHV02027.1, ECO:0000313|Proteomes:UP000179734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MO-5499 {ECO:0000313|EMBL:OHV02027.1}, and NE-TNMC-100812
RC {ECO:0000313|Proteomes:UP000179734};
RA Greninger A.L., Elliott B., Vasireddy S., Vasireddy R.;
RT "Genome sequence of Mycobacterium talmonii.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PQM49002.1, ECO:0000313|Proteomes:UP000238296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2683 {ECO:0000313|EMBL:PQM49002.1,
RC ECO:0000313|Proteomes:UP000238296};
RX PubMed=28809146; DOI=10.1099/ijsem.0.001998;
RA Davidson R.M., DeGroote M.A., Marola J.L., Buss S., Jones V., McNeil M.R.,
RA Freifeld A.G., Elaine Epperson L., Hasan N.A., Jackson M., Iwen P.C.,
RA Salfinger M., Strong M.;
RT "Mycobacterium talmoniae sp. nov., a slowly growing mycobacterium isolated
RT from human respiratory samples.";
RL Int. J. Syst. Evol. Microbiol. 67:2640-2645(2017).
RN [3] {ECO:0000313|EMBL:PQM49002.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-2683 {ECO:0000313|EMBL:PQM49002.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OHV02027.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MLQM01000092; OHV02027.1; -; Genomic_DNA.
DR EMBL; PPEA01000110; PQM49002.1; -; Genomic_DNA.
DR RefSeq; WP_071027681.1; NZ_MLQM01000092.1.
DR AlphaFoldDB; A0A1S1NH41; -.
DR Proteomes; UP000179734; Unassembled WGS sequence.
DR Proteomes; UP000238296; Unassembled WGS sequence.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd04410; DMSOR_beta-like; 1.
DR Gene3D; 3.30.70.20; -; 1.
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; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF91; NADPH:ADRENODOXIN OXIDOREDUCTASE, MITOCHONDRIAL; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:PQM49002.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000179734}.
FT DOMAIN 1..29
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 37..66
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 561 AA; 59892 MW; BC3FF41E0A74707F CRC64;
MPHVITQACC NDASCVFACP VNCIHPTPDE PGFATSEMLY IDPVACVDCG ACVRACPVEA
IAPDTRLAPK QQPFIAINAA HYPDRPAGVK LPPTSKLAPV LPAAEIRHGR YPLTVAIVGS
GPAAMYAADE LLTQPGVLVN MFEKLPTPYG LVRAGVAPDH QRTKLVTRLF DKVAAHRRFN
FFLNVEVGNH LSHADLLAHH HAVLYASGAP NDRRLRIDGM ELPGTGTATE LVAWINGHPE
FTDLPVDLSG ERVVIVGNGN VAFDVARVLT ADPDELARTD ISDNALAALR DSRVQEVVIV
ARRGPAASAF TLPELIGLTQ TAEVVLDAAD HDRVRRDLAT TDSALTRRKL EILSKLGDAS
APITRPRIRL AYELTPKRVI GPQRVTAMEF TRTGTDAVET LPAGLVLTSI GYHGKAIADL
PFDDDAGVVP NDAGRVVDPA SGQPVPGAYV SGWIKRGPTG FIGTNKSDSL QTVHTLVADY
NAGRLGELAG GPRAIARLVH ARQPEVIDAA GWKAIDAAEI ARGAADGRPR DKFVDIRDML
AAAASAPPEP LHRRLLNLVQ R
//
