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Database: UniProt
Entry: A0A1E7JZG8_9ACTN
LinkDB: A0A1E7JZG8_9ACTN
Original site: A0A1E7JZG8_9ACTN 
ID   A0A1E7JZG8_9ACTN        Unreviewed;       470 AA.
AC   A0A1E7JZG8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Fumarate reductase {ECO:0000313|EMBL:OEU97050.1};
GN   ORFNames=AN216_17525 {ECO:0000313|EMBL:OEU97050.1};
OS   Streptomyces oceani.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1075402 {ECO:0000313|EMBL:OEU97050.1, ECO:0000313|Proteomes:UP000176101};
RN   [1] {ECO:0000313|EMBL:OEU97050.1, ECO:0000313|Proteomes:UP000176101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 02100 {ECO:0000313|EMBL:OEU97050.1,
RC   ECO:0000313|Proteomes:UP000176101};
RX   PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA   Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA   Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT   "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT   Adaptation to the Marine Environment and Their Diversity at the Genomic
RT   Level.";
RL   Front. Microbiol. 7:998-998(2016).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OEU97050.1}.
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DR   EMBL; LJGU01000132; OEU97050.1; -; Genomic_DNA.
DR   RefSeq; WP_070197610.1; NZ_LJGU01000132.1.
DR   AlphaFoldDB; A0A1E7JZG8; -.
DR   STRING; 1075402.AN216_17525; -.
DR   PATRIC; fig|1075402.3.peg.2487; -.
DR   OrthoDB; 9813348at2; -.
DR   Proteomes; UP000176101; Unassembled WGS sequence.
DR   GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176101}.
FT   DOMAIN          9..427
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   REGION          450..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  48947 MW;  04C6C5026D57B0A3 CRC64;
     MSVENTDVDV VVVGAGGGGL TAAIAAAETG ASVALLEKLD RPGGNTFVST GSIPAGGTRY
     QRAAGIEDDA ERMTADLLRQ SGDHEAEHLV RFLAEESAGL VEWLVERHDV DLRIITDYKH
     VGHSVQRLHA PPDRRGESLI RDLSAAARRL DVEIVVGNPV AGLLVEDGRV SGVRVAGERS
     GSYELRSHAV VLAGNGFGNN QQMIDRWLPE ASAAQYFGAD GSTGENITWA TDLGARLLNM
     GAYQGYAAVA YPHGSIVSWT SVEKGGFLLA PDGHRMGDES VGYSGFASEV AKVAEESWVV
     FDTRIRDFIA GNEPEFAELV TIGGVKEATS ATALAEIIGC SATAVEAAIT DQQRAAASGT
     ADATGRRDFP MGPLKEPYCA VRSVPALFHT QGGVDVDRYA RVIRQDGTTV PGLHAVGGVT
     GGLSGRSGGR GYSSGNGLLS AVGLGRVAGS TAARRPGRPA PHADRDPDGP
//
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