ID L0AAC8_CALLD Unreviewed; 443 AA.
AC L0AAC8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=NAD(FAD)-dependent dehydrogenase {ECO:0000313|EMBL:AFZ70379.1};
GN OrderedLocusNames=Calag_0624 {ECO:0000313|EMBL:AFZ70379.1};
OS Caldisphaera lagunensis (strain DSM 15908 / JCM 11604 / ANMR 0165 /
OS IC-154).
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Caldisphaeraceae;
OC Caldisphaera.
OX NCBI_TaxID=1056495 {ECO:0000313|EMBL:AFZ70379.1, ECO:0000313|Proteomes:UP000010469};
RN [1] {ECO:0000313|Proteomes:UP000010469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15908 / JCM 11604 / IC-154
RC {ECO:0000313|Proteomes:UP000010469};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete genome of Caldisphaera lagunensis DSM 15908.";
RL Submitted (MAR-2012) 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; CP003378; AFZ70379.1; -; Genomic_DNA.
DR RefSeq; WP_015232277.1; NC_019791.1.
DR AlphaFoldDB; L0AAC8; -.
DR STRING; 1056495.Calag_0624; -.
DR GeneID; 14211884; -.
DR KEGG; clg:Calag_0624; -.
DR eggNOG; arCOG01069; Archaea.
DR HOGENOM; CLU_003291_1_3_2; -.
DR InParanoid; L0AAC8; -.
DR OrthoDB; 27922at2157; -.
DR Proteomes; UP000010469; Chromosome.
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:UP000010469}.
FT DOMAIN 6..286
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 325..428
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 443 AA; 49686 MW; 7B94A6F8F85D4B2D CRC64;
MNKETLAIIG GGDAGMTTAS WARRRKPHMN IIVFEKTNLI SHAPCGLPYF IEGLFDDEKL
LSAYTPEEFE KERNVNIRIN HEIIELDLDN RVIYAKNRNN NDIIKLEYDY LAIATGSKPK
KIKYDNESRI FYVHHPSLAR EVKEKIMNLN NVAIIGGGIL GVELAEALVR NGKNVLLIHK
NAYLLNKMLD NDMASYINNY VSKDIKLKLN EEVLEITDGG RVIITNNGKY EVDGTIVSIG
VEPNTELIND KNMIGETKAI KTDEYMRTSY KDVYAVGDVA ESTNIITGMP DWQPFAPVAG
KMGFTAGNHI GGVNYRFPGL IGTAITKYGE YFIAKTGLTE NEAKKYGFKT ISTIIRSNTR
ARYYPGGKEI IIKLIADENT QKLIGAQIIG QEEVLGRIDL LALAIMKSNT LYDLFYLEHA
YMPAISRSWD PVILAARSLL TKF
//
