ID E2AHG9_CAMFO Unreviewed; 537 AA.
AC E2AHG9;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Thioredoxin reductase 1, mitochondrial {ECO:0000313|EMBL:EFN67124.1};
GN ORFNames=EAG_12107 {ECO:0000313|EMBL:EFN67124.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN67124.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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DR EMBL; GL439539; EFN67124.1; -; Genomic_DNA.
DR AlphaFoldDB; E2AHG9; -.
DR STRING; 104421.E2AHG9; -.
DR EnsemblMetazoa; XM_011259803.3; XP_011258105.1; LOC105252447.
DR InParanoid; E2AHG9; -.
DR OMA; CFDYVKP; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; 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; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR NCBIfam; TIGR01438; TGR; 1.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF6; THIOREDOXIN REDUCTASE 2; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 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.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..537
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003157199"
FT DOMAIN 54..388
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 408..518
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 510
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 109
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 175
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 240..247
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 331
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 372
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 100..105
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 537 AA; 58569 MW; 680FD73872EB7456 CRC64;
MATLAVFTRL LSLRGAHAKL FGLPRWHPTL VKCDDLIYGG SAMACMCTEQ KYTYDLLVIG
GGSGGLAAAK EAVGLNAKVA VLDYVTPSPL GTTWGLGGTC VNVGCIPKKL MHQAALLGEA
VHEAATFGWQ LPDPKTVKIN WEALKTAVQN HVKSVNWVTR VELRTKKVDY FNALGHFMDA
HTVVGVTKKG EEKVFTAKNI LIAVGGRPRY PDIPGALEYG ISSDDIFSLE RAPGKTLVVG
AGYIGLECAG FLNGLGYDTT IMVRSIVLRG FDQQMANLVA EEMEQRGVHF IYQAKPKKVA
KQEDGRLLVD WVDKDGQIHQ DVYDTVLFAI GRRALTEELK PENAGLKLVP ETNKIEAINE
QTNVPNIYAV GDVLHKRPEL TPVAIHAGKL LARRLFDNST EQMDYTNVAT TVFSPLEYGC
VGLSEEAAIG LHGEEEIEIY HAYYKPTEFF VPQKDVDRCY VKVVAFRSGD QRVLGIHFVG
PNAGEVIQGF AAAIKCGLTI PKLKATVGIH PTVAEEFTRI SVTKRSGLDP KPQSCCS
//
