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Database: UniProt
Entry: A2SP72_METPP
LinkDB: A2SP72_METPP
Original site: A2SP72_METPP 
ID   A2SP72_METPP            Unreviewed;       425 AA.
AC   A2SP72;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Putative ferredoxin reductase {ECO:0000313|EMBL:ABM97361.1};
GN   OrderedLocusNames=Mpe_B0597 {ECO:0000313|EMBL:ABM97361.1};
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OG   Plasmid RPME01 {ECO:0000313|EMBL:ABM97361.1,
OG   ECO:0000313|Proteomes:UP000000366}.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM97361.1, ECO:0000313|Proteomes:UP000000366};
RN   [1] {ECO:0000313|EMBL:ABM97361.1, ECO:0000313|Proteomes:UP000000366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC   {ECO:0000313|Proteomes:UP000000366};
RC   PLASMID=RPME01 {ECO:0000313|EMBL:ABM97361.1,
RC   ECO:0000313|Proteomes:UP000000366};
RX   PubMed=17158667; DOI=10.1128/JB.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP000556; ABM97361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2SP72; -.
DR   KEGG; mpt:Mpe_B0597; -.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_003291_4_0_4; -.
DR   BioCyc; MetaCyc:MONOMER-19841; -.
DR   Proteomes; UP000000366; Plasmid RPME01.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; 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   Plasmid {ECO:0000313|EMBL:ABM97361.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000366}.
FT   DOMAIN          14..311
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          332..409
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   425 AA;  44982 MW;  7161CD8231544A18 CRC64;
     MISTAQERGD TRAILVLGAG QAGFQVAASL RDFGYRGCVT LVGDEPHWPY RRPPLSKGYL
     EGSDSAGTLA LRLGANQESL ELVMRLGKKG LAIDRSSNIV TLDSGERIGY DHLVIAMGAT
     PRALRVPGVH LEGVLSLRTV EHAEALRNLF REPGDMVVIG GGFIGMEVAA VAAKAGQRVT
     VVEAEDRVMS RVVAPEISGY VASEHAAHGV SIMTGRCAVA FHGRSGRVSA VELDDGVRLP
     ARIVLVGVGV SPNIALAEEA ALTVDNGIVV DGSLLTSDER ISAIGDCSSF PSVHARRRVR
     LESVQNAVDQ AKYVAGRLTG MMGEVYQGTP CFWTRQYSTS IQIAGIGDGN DERWVSGDPA
     SGKFSIFRFN GGTLSCVESV NSSADHAAVR KLFSGGMPLP TPRELTDAQF LPKLSLERVA
     AAESS
//
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