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Database: UniProt
Entry: C9Z4A3_STRSW
LinkDB: C9Z4A3_STRSW
Original site: C9Z4A3_STRSW 
ID   C9Z4A3_STRSW            Unreviewed;       511 AA.
AC   C9Z4A3;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Putative iron-sulfur binding oxidoreductase {ECO:0000313|EMBL:CBG72853.1};
GN   OrderedLocusNames=SCAB_58311 {ECO:0000313|EMBL:CBG72853.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG72853.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG72853.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG72853.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
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DR   EMBL; FN554889; CBG72853.1; -; Genomic_DNA.
DR   RefSeq; WP_013003420.1; NC_013929.1.
DR   AlphaFoldDB; C9Z4A3; -.
DR   STRING; 680198.SCAB_58311; -.
DR   GeneID; 24312173; -.
DR   KEGG; scb:SCAB_58311; -.
DR   eggNOG; COG0665; Bacteria.
DR   eggNOG; COG0723; Bacteria.
DR   HOGENOM; CLU_007884_15_1_11; -.
DR   Proteomes; UP000001444; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR   PANTHER; PTHR13847:SF274; RIESKE 2FE-2S IRON-SULFUR PROTEIN YHFW-RELATED; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT   DOMAIN          426..511
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   511 AA;  55439 MW;  A7FE40F9613C0FED CRC64;
     MQPEEHTRPE QRSYWIESAP HEGEHPAPDG DLVVDVAVVG AGIAGISTAW ELARRGRRVA
     LLEADRVAAG VTGHTTAKVT ALHTLVYDRL RRTRGAEAAA LYAQSQSEAI RHAAAVVEEL
     GIACDWEDAA AYTYAEDEGR VAELRAEAEA AREAGLPAEF VTETGLPFPV AGAVRVADQA
     QFHPRRYLLA LVGDLVRLGA SVHERTRVTR LKEGSPCRLT TDAGYTVTAE DVVVATHYPV
     FDRALLFTRL SPRRELVLAA PVPADADPHG MYITQEQRTR SARTAPYGDG QRLLIVTGEH
     FTPGTAGVEE RFELLAEWAV ERFGPLGFTH RWATQDNDST DSVPLVGPFH AGSRHTWVAT
     GFGGWGMSGG IMAGRLLAES ITGHKSAWSD LYDPRRVLSA VREAPSFLKH QAQVARHFVG
     DRISPPGNAS VDAIAPGDGA VVRVGAHHHA VHRDEDGSLH AVSARCTHMG CLVGFNRAER
     TWECPCHGSR FDVEGRIVQG PATKPLERRD I
//
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