ID F8DEB7_HALXS Unreviewed; 448 AA.
AC F8DEB7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:AEH39399.1};
DE EC=1.8.1.14 {ECO:0000313|EMBL:AEH39399.1};
GN OrderedLocusNames=Halxa_0156 {ECO:0000313|EMBL:AEH39399.1};
OS Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6).
OG Plasmid pHALXA02 {ECO:0000313|EMBL:AEH39399.1,
OG ECO:0000313|Proteomes:UP000006794}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halopiger.
OX NCBI_TaxID=797210 {ECO:0000313|EMBL:AEH39399.1, ECO:0000313|Proteomes:UP000006794};
RN [1] {ECO:0000313|Proteomes:UP000006794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18323 / JCM 14033 / SH-6
RC {ECO:0000313|Proteomes:UP000006794};
RC PLASMID=Plasmid pHALXA02 {ECO:0000313|Proteomes:UP000006794};
RX PubMed=22675596; DOI=10.4056/sigs.2505605;
RA Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A.,
RA Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N.,
RA Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., Klenk H.P.,
RA Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Halopiger xanaduensis type strain (SH-6(T)).";
RL Stand. Genomic Sci. 6:31-42(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR EMBL; CP002841; AEH39399.1; -; Genomic_DNA.
DR RefSeq; WP_013881940.1; NC_015667.1.
DR AlphaFoldDB; F8DEB7; -.
DR GeneID; 10799489; -.
DR KEGG; hxa:Halxa_0156; -.
DR eggNOG; arCOG01069; Archaea.
DR HOGENOM; CLU_003291_1_3_2; -.
DR OrthoDB; 27922at2157; -.
DR Proteomes; UP000006794; Plasmid pHALXA02.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050451; F:CoA-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:AEH39399.1};
KW Plasmid {ECO:0000313|EMBL:AEH39399.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006794}.
FT DOMAIN 5..300
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 330..431
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 448 AA; 47047 MW; 0117BC5CEDB9B392 CRC64;
MSDTFVVVGG DAAGMSAASK AKREDPSCDV IVFEKGKWVS YAACGMPYYV KGEVDELDDL
VAVTPEEFRE ERDIDLRTAA EVVDIDREAR TVTVKTSKGT EEQPYDDLLI ATGASAIEPP
FDGLGHEGVF TIHDMDEADA IEDYVTGRDP ETAAIVGGGY VGIEMAEALS TRGVDVHLYE
MLPHVLQPFG EAVAEVVEDH LREQGVDLHL ETAVSGFGGD DRVGTVELED ETVPADVAIV
GVGVAPNTDL AERAGIELGP TGAIATDEYG RTNDRHVYAA GDCAEATNVV TGEPDHVPLA
LTANRAGRAI GQTVTGDPTP TGGTAGTAIV KAFELGAART GIVDEDQARE AGFDPVSVTI
SASTRAHYYP DGAELTVTLV ADRESGRLLG GTVVGREGAK RIDTVATALT SGMTVSELQN
TDLAYAPPFS PVWDPILTAA KVLNGKLE
//
