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
//