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Database: UniProt
Entry: A0A089XGP3_STRGA
LinkDB: A0A089XGP3_STRGA
Original site: A0A089XGP3_STRGA 
ID   A0A089XGP3_STRGA        Unreviewed;       465 AA.
AC   A0A089XGP3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:AIS01102.1};
GN   ORFNames=SGLAU_25820 {ECO:0000313|EMBL:AIS01102.1};
OS   Streptomyces glaucescens.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1907 {ECO:0000313|EMBL:AIS01102.1, ECO:0000313|Proteomes:UP000029482};
RN   [1] {ECO:0000313|Proteomes:UP000029482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40922 / GLA O {ECO:0000313|Proteomes:UP000029482};
RX   PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA   Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA   Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of the actinobacterium Streptomyces glaucescens
RT   GLA.O (DSM 40922) consisting of a linear chromosome and one linear
RT   plasmid.";
RL   J. Biotechnol. 194:81-83(2015).
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; CP009438; AIS01102.1; -; Genomic_DNA.
DR   RefSeq; WP_043504809.1; NZ_CP009438.1.
DR   AlphaFoldDB; A0A089XGP3; -.
DR   STRING; 1907.SGLAU_25820; -.
DR   KEGG; sgu:SGLAU_25820; -.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_003291_1_3_11; -.
DR   OMA; ACGIPYW; -.
DR   OrthoDB; 9802028at2; -.
DR   Proteomes; UP000029482; 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; NAD(P)H SULFUR OXIDOREDUCTASE (COA-DEPENDENT); 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   Reference proteome {ECO:0000313|Proteomes:UP000029482}.
FT   DOMAIN          12..310
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          344..445
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   465 AA;  49178 MW;  6AD5B7221AF552DB CRC64;
     MDMSRTRSTR QRLVVIGGDA AGMSAASQAR RLRGPEELEI VAFERGHFTS YSACGIPYWV
     GGDVAGRDEL IARTPEEHRA RGIDLRLRTE VTAIDPAGRR VRARDLGSGT ESWTSYDHLV
     IATGARPVRP DLPGADAPGV HGVQTLDDGQ ALLDTLTRTR GRRAVVVGAG YIGVEMAEAL
     IHRGYEVTVL NRGGAPMSTL DPDMGRLVRD AMSGMGITMV DDAEVTKVLT GDDGRVRAVA
     TQDAEYPADV VVLGIGVRPD TALARAAGLP LGDNGGLLTD LAMRVRGHED IWAGGDCVEV
     LDLVSGRERH IPLGTHANKH GQVIGTNIGG GYATFPGVVG TAVSKVCDLE IARTGLREKD
     ARRAGLQYVA VTIESTSRAG YYPGASPMTV KMLAERRTGR LLGVQIVGRE GAGKRVDIAA
     VALTAGLTVE QVAHLDLGYA PPFSPVWDPV QVAARKAVAA VREAP
//
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