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Database: UniProt
Entry: H1KII6_METEX
LinkDB: H1KII6_METEX
Original site: H1KII6_METEX 
ID   H1KII6_METEX            Unreviewed;       413 AA.
AC   H1KII6;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Ferredoxin--NAD(+) reductase {ECO:0000313|EMBL:EHP92650.1};
DE            EC=1.18.1.3 {ECO:0000313|EMBL:EHP92650.1};
GN   ORFNames=MetexDRAFT_2448 {ECO:0000313|EMBL:EHP92650.1};
OS   Methylorubrum extorquens DSM 13060.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=882800 {ECO:0000313|EMBL:EHP92650.1, ECO:0000313|Proteomes:UP000004382};
RN   [1] {ECO:0000313|EMBL:EHP92650.1, ECO:0000313|Proteomes:UP000004382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13060 {ECO:0000313|EMBL:EHP92650.1,
RC   ECO:0000313|Proteomes:UP000004382};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Koskimaki J., Halonen O., Pirttila A.,
RA   Frank C., Woyke T.J.;
RT   "The draft genome of Methylobacterium extorquens DSM 13060.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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:EHP92650.1}.
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DR   EMBL; AGJK01000054; EHP92650.1; -; Genomic_DNA.
DR   RefSeq; WP_003599930.1; NZ_AGJK01000054.1.
DR   AlphaFoldDB; H1KII6; -.
DR   PATRIC; fig|882800.3.peg.2396; -.
DR   Proteomes; UP000004382; Unassembled WGS sequence.
DR   GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR028202; Reductase_C.
DR   PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:EHP92650.1}.
FT   DOMAIN          7..310
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          329..411
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   413 AA;  43298 MW;  F5DA5424FB00AFFA CRC64;
     MSGPMETIVI VGAGQAGFQA AASLREAGFS GRLTLVGEEA ALPYQRPPLS KAYLAGKTDA
     RGLLLRQESF FAEHRIEHRP GTRVTAIDRA GRSVRLSDGE DLSYDHLILA TGTRNRALPV
     PGADLDGVRQ LRSLDDADAL RAAIEGIHRI VVVGAGFIGL EFAAVCAARG LSVTVIEAAE
     RVMARAVSPE TSEAFRAFHE EAGVTFLFGA GVTAIEGEGG RAVAVRTADG QSLPADLVLV
     GIGVVPNQEL AEEVGLAVRD GIEIDAFLAT SDPAISAIGD CVRFPSRFAS GMPGGDRVRI
     ESVQNAVDQG RCLAARLTGR PAAYDAVPWF WSDQGPRKLQ IAGLAAPSDA SVLRRAGAGF
     SVFRFRDGAL TAVESVDRPA DHMAARRLLA AGKRLTPEQA GDPGFDLKAL ATG
//
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