ID C4RQD8_MICS3 Unreviewed; 457 AA.
AC C4RQD8;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Pyridine nucleotide-disulphide oxidoreductase dimerization region {ECO:0000313|EMBL:EEP71478.1};
GN ORFNames=MCAG_01805 {ECO:0000313|EMBL:EEP71478.1};
OS Micromonospora sp. (strain ATCC 39149 / NRRL 15099 / SCC 1413).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=219305 {ECO:0000313|EMBL:EEP71478.1, ECO:0000313|Proteomes:UP000010307};
RN [1] {ECO:0000313|Proteomes:UP000010307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39149 / NRRL 15099 / SCC 1413
RC {ECO:0000313|Proteomes:UP000010307};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Galagan J., Nusbaum C., Birren B.;
RT "The genome sequence of Micromonospora carbonacea var. africana strain ATCC
RT 39149.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR EMBL; GG657738; EEP71478.1; -; Genomic_DNA.
DR RefSeq; WP_007072754.1; NZ_GG657738.1.
DR AlphaFoldDB; C4RQD8; -.
DR STRING; 219305.MCAG_01805; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_3_11; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000010307; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000010307}.
FT DOMAIN 4..298
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 336..438
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 457 AA; 48459 MW; 8A0DA9631D6CE39C CRC64;
MAQRLIIIGG DAAGMSAASQ ARRRRDRADL EIVAFERGNF TSYSACGIPY WISGVVPEQH
QLVARDPATF RTDFDIDVRL RHEVTAIDLD RREVVARDLD GGGEVRERFD DLVYATGAVP
KRPDWADPGV RGVFGVQTLD DASALREWLD ADPAPRRAVV VGGGYIGVEM AESLIQRGLS
VTLVEQAHQP MSTVDADMAA LVADAMRGVG IDIRTGVEVT GLDGRDGRVS AVVTADGPLP
ADVVVLGLGV RPNTALAEAA GLPVGPSGAI RVDRRMRVPG VPGVWAAGDC VETLHRVSGL
PVHVPLGTHA NKQGRVAGIN LGGGYATFPG VIGTAVTKVC NLEVGRTGLR ERDAAASGFE
FVSVLSESTN RAGYYPGART MTVKLIAERP SGRLLGAQIV GWSEAAKRID TLAVALWNEM
TVDEMTALDL GYAPPYAPVW DPVLIAARKA VDALHRG
//
