ID A0A934P750_9NOCA Unreviewed; 555 AA.
AC A0A934P750;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 02-APR-2025, entry version 10.
DE RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN ORFNames=JGU72_25090 {ECO:0000313|EMBL:MBJ8347963.1};
OS Antrihabitans sp. YC2-6.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Nocardiaceae; Antrihabitans.
OX NCBI_TaxID=2799498 {ECO:0000313|EMBL:MBJ8347963.1, ECO:0000313|Proteomes:UP000620813};
RN [1] {ECO:0000313|EMBL:MBJ8347963.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YC2-6 {ECO:0000313|EMBL:MBJ8347963.1};
RA Lee S.D., Kim I.S.;
RT "Antrihabitans popcorni sp. nov. and Antrihabitans auranticaus sp. nov.,
RT isolated from a larva cave.";
RL Submitted (DEC-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 ECO:0000256|PIRSR:PIRSR000362-1};
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008312}.
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:MBJ8347963.1}.
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DR EMBL; JAEMNW010000007; MBJ8347963.1; -; Genomic_DNA.
DR RefSeq; WP_199686825.1; NZ_JAEMNW010000007.1.
DR Proteomes; UP000620813; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; 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 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 InterPro; IPR021163; Ferredox_Rdtase_adrenod.
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 PIRSF; PIRSF000362; FNR; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000362-1};
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, ECO:0000256|PIRSR:PIRSR000362-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000620813}.
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"
FT BINDING 117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 137
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 145
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 252..255
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 296..297
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 308
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
FT BINDING 463
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 470..472
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-1"
FT BINDING 470
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000362-2"
SQ SEQUENCE 555 AA; 60353 MW; 3CEF20A355B4DB21 CRC64;
MAYVITQRCC NDASCITECP VDCIRPSPKD PDFTTTEMLY IDPQTCIDCG ACVDACPVDA
IFSEDELSKS LERFRDINAA YFDRHPLEPD MSPLAIPVRP DKSLGTLRVA VIGAGPAACY
SADELLKRAD VEVEMLEKLP TPYGLVRAGV APDHPGTKGV TSMFESSFKR QTFQYYLNVE
VGKHISHAEL LQHHHAVVYA VGASSDRHLG VPGEDLPGSH AATEFVAWYN GHPEYADRTF
DLSGERAIIV GNGNVALDVA RVLTLGPDEL AKTDIADHAL EALRNSNIRE VVLLGRRGPA
QAAYTSSEFL ALGYLKNIDV IVDEEDLVLD DASQAAVDDP DAEPSLRLKV ALAKEYAAKS
ADPARKRIVL RYLVSPAEVL GSDKVEGVRI VKNTLVESAR GLDAQPTDET ETIDAGLVIR
SIGYRGVAIE DLPYDERSGT VPNENGRVVV DGEPVRGVYV SGWIKRGPRG VIGSNKTDAE
ETIHLLLEDF MAGRLEAPTG GRAELAKLLA DRQKDIVGRD GWRAIDTEER KRGKDAGRPR
VKFTSVDELL QAAKG
//
