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Database: UniProt
Entry: A0A7W7CEJ5_9PSEU
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ID   A0A7W7CEJ5_9PSEU        Unreviewed;       502 AA.
AC   A0A7W7CEJ5;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   02-APR-2025, entry version 14.
DE   RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE            EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN   ORFNames=HNR67_005768 {ECO:0000313|EMBL:MBB4679650.1};
OS   Crossiella cryophila.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Crossiella.
OX   NCBI_TaxID=43355 {ECO:0000313|EMBL:MBB4679650.1, ECO:0000313|Proteomes:UP000533598};
RN   [1] {ECO:0000313|EMBL:MBB4679650.1, ECO:0000313|Proteomes:UP000533598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44230 {ECO:0000313|EMBL:MBB4679650.1,
RC   ECO:0000313|Proteomes:UP000533598};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 reduced [2Fe-2S]-[ferredoxin] + NADP(+) + H(+) = 2 oxidized
CC         [2Fe-2S]-[ferredoxin] + NADPH; 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:ARBA00047776};
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:MBB4679650.1}.
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DR   EMBL; JACHMH010000001; MBB4679650.1; -; Genomic_DNA.
DR   RefSeq; WP_185005372.1; NZ_BAAAUI010000001.1.
DR   AlphaFoldDB; A0A7W7CEJ5; -.
DR   Proteomes; UP000533598; 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   InterPro; IPR055275; Ferredox_Rdtase.
DR   PANTHER; PTHR48467; GLUTAMATE SYNTHASE 1 [NADH], CHLOROPLASTIC-LIKE; 1.
DR   PANTHER; PTHR48467:SF1; GLUTAMATE SYNTHASE 1 [NADH], CHLOROPLASTIC-LIKE; 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; 1.
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:MBB4679650.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000533598}.
FT   DOMAIN          37..66
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   502 AA;  53189 MW;  7A56C2555277E940 CRC64;
     MAFAITQTCC ADASCITVCP VNCIHPTPDE PDFGRTDLLY VDPSACIDCG ACADACPVDA
     IFPVAELPAD LKPYARINAD YYTDRAPAET APAPMFHAWS PPEFSRTIPA DFAPLDIAVV
     GTGPAGMYTV ADLLLHTNAR VTLIDRLPVT GGLIRYGVAP DHPSTKKIAE TFARFHQHPR
     LTLRLGVQIG RDITPAELSA QHDAVIYAVG ASAARTLDIP GEHLPGSLAA TTVVAWYNGH
     PDIPATAVDL SAERVVLVGN GNVALDVARI LTADPNTLAD TTTAPTALTQ LTSSKVREVV
     VLARRGPADA AYTMPELLAL TERADIDLVL DDQDPRTTHA VDASEGKAAL LQGITRQTVD
     WSTPPAPGRR RIVLRFHSTP LEIVGDTEVR GLRVTGPDGE IEIATGQVIR AVGYRGNPLP
     GLPFDPATGT IPHERGRVSP GTYVVGWIKR GPTGGIGANK SCASETVGTL LTDAIATTLP
     PRTPRPTRLT RLTSLLRGRP TT
//
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