ID E1RFR8_METP4 Unreviewed; 389 AA.
AC E1RFR8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ADN37372.1};
GN OrderedLocusNames=Mpet_2629 {ECO:0000313|EMBL:ADN37372.1};
OS Methanolacinia petrolearia (strain DSM 11571 / OCM 486 / SEBR 4847)
OS (Methanoplanus petrolearius).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanolacinia.
OX NCBI_TaxID=679926 {ECO:0000313|EMBL:ADN37372.1, ECO:0000313|Proteomes:UP000006565};
RN [1] {ECO:0000313|EMBL:ADN37372.1, ECO:0000313|Proteomes:UP000006565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11571 / OCM 486 / SEBR 4847
RC {ECO:0000313|Proteomes:UP000006565};
RX PubMed=21304750;
RA Brambilla E., Djao O.D., Daligault H., Lapidus A., Lucas S., Hammon N.,
RA Nolan M., Tice H., Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA Spring S., Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Methanoplanus petrolearius type strain (SEBR
RT 4847).";
RL Stand. Genomic Sci. 3:203-211(2010).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CP002117; ADN37372.1; -; Genomic_DNA.
DR AlphaFoldDB; E1RFR8; -.
DR STRING; 679926.Mpet_2629; -.
DR KEGG; mpi:Mpet_2629; -.
DR eggNOG; arCOG01297; Archaea.
DR HOGENOM; CLU_031864_5_3_2; -.
DR Proteomes; UP000006565; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:UniProt.
DR CDD; cd02976; NrdH; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR48105:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000006565}.
FT DOMAIN 10..69
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
FT DOMAIN 91..375
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 389 AA; 42408 MW; 18918325EFE47C29 CRC64;
MEKAVTMPDV KVYSTKQCQY CRLLKAFLDK KGIKYQNIDV GEDIEAAKEM VELSGQYAVP
VTVIDGEVIV GYDVRRLNEL FGDTGEKGEI DIIILGGGPA GLTAAAYAAR KLLRCMIITE
DIGGQALESW AIENYMGFRI ISGSDLMQKF EEQVRNEDIE IEIDRAESIE ESNGKFVITT
VSGQKFEGKS VIIATGVKPR WLGIKDEEKY IGHGISICST CDGPLFRDKI VTIVGGGNYA
VTTAIEMSKL ATHVNLIVRS KIRADEVYTS QYEGLENVST YKNYTVSALE GDNMLKAVTI
KERDTGEESK LETDGLFLAI GHDANTGFLE GFVDLNENGE IITDNNGRTS HNGVFAAGDV
TDTKSKQVII ASGEGAKAAL SAYSFLVNK
//