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Database: UniProt
Entry: J9SAD9_9ACTN
LinkDB: J9SAD9_9ACTN
Original site: J9SAD9_9ACTN 
ID   J9SAD9_9ACTN            Unreviewed;      1197 AA.
AC   J9SAD9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Fe-S oxidoreductase {ECO:0000313|EMBL:AFR50811.1};
GN   ORFNames=KTR9_4204 {ECO:0000313|EMBL:AFR50811.1};
OS   Gordonia sp. KTR9.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR50811.1, ECO:0000313|Proteomes:UP000003281};
RN   [1] {ECO:0000313|EMBL:AFR50811.1, ECO:0000313|Proteomes:UP000003281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KTR9 {ECO:0000313|EMBL:AFR50811.1,
RC   ECO:0000313|Proteomes:UP000003281};
RX   PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA   Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA   Indest K.J., Eltis L.D.;
RT   "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT   trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL   Appl. Environ. Microbiol. 78:7798-7800(2012).
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DR   EMBL; CP002907; AFR50811.1; -; Genomic_DNA.
DR   RefSeq; WP_014928246.1; NC_018581.1.
DR   AlphaFoldDB; J9SAD9; -.
DR   STRING; 337191.KTR9_4204; -.
DR   KEGG; gor:KTR9_4204; -.
DR   PATRIC; fig|337191.3.peg.4599; -.
DR   eggNOG; COG0247; Bacteria.
DR   HOGENOM; CLU_005304_0_1_11; -.
DR   Proteomes; UP000003281; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   PANTHER; PTHR43255:SF6; IRON-SULFUR-BINDING OXIDOREDUCTASE FADF-RELATED; 1.
DR   PANTHER; PTHR43255; IRON-SULFUR-BINDING OXIDOREDUCTASE FADF-RELATED-RELATED; 1.
DR   Pfam; PF02754; CCG; 2.
DR   Pfam; PF13187; Fer4_9; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        73..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        219..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          290..320
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          406..438
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          766..1197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        915..929
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        981..1005
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1121..1137
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1159..1173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1197 AA;  125866 MW;  EEC6EF52CF8F6DF8 CRC64;
     MTTTTIAIGT TAAVISLFCW YLFLGGVVRI YRTIKLGHKV DSSRFWPILP RMMTMLKEFI
     VHTRMVKFRT VGWAHWLVMV GFLGGFLLWF EAYGQSINPE FHWPVFGDTF AWHLWDELLG
     IATVVGIIVL IVIRQLNHPR VPERLSRFGG SRFGPAYFVE GVVLLEGLGM ILVKASKIAT
     YGHANVYSDF FTMQVAKILP ASPTLVSIFA VIKLMSGMVW LAMVGMNISW GVAWHRFSAF
     FNIYFKREQD GGVALGAAKP MMSQGKVLDM ETADPDVDAF GAGKIEDFSW KGWLDFTTCT
     ECGRCQSQCP AWNTGKPLSP KLLIMSLRDH GNAKAPYLLA GGRKDMGGDE VGLVDADGNV
     DEDKLNAIPE AARAEAARKL VGESKGDLGG GQVVEAVEGE FDPEALGAVI DTETLWSCTT
     CGACVEQCPV DIEHVDHILD MRRYQVLIES DFPTELAGMF KNLENKGNPW GQNASARTAW
     IDEMDIEIPV FGKDVESFEG FEYLFWVGCA GAYEDRAKKT TKAVAELLDM AAVNFMVLGE
     GETCTGDSAR RAGNEFLFQM LAQQNIEMLG EVFATAPDQR KKVVVTCAHC FNALGNEYPQ
     LGAKYEVVHH TQLLNRLVRD KRLVPVAPLG EGVTYHDPCY LGRHNKVYDA PRELMGAAGS
     TLTEMPRHGE RSMCCGAGGA RMWMEEQIGK RINLDRVDEA LDTLGDTTGD QVKKVATGCP
     FCRVMLTDGV TARTSGTESE GKVEVVDVAQ LLLESVKRDR TEVKLGGRFL GPRPTVAEPE
     PEPEPEKVPA AATASASATT EAAPKPKVGL GMKGGKKPGA TAKTAAPEAP AEKAPAEKKP
     ASKGFGMKGG KKPGAAASSA APATDSAPAE APAEAPAEKK PAAKGFGMKG GAKRPGAAGK
     PAGGTAQPVP AETESSEAVK EEVAEAATET AAEKKPASKG FGMGKAKRPG QKTTNAAAPA
     AGVTAPAESK VDESESAPDA APTVDTESAT AGTATTETAT AETSVAAATE EKPGKAKGFG
     MSAGKKRPGG IGKSAAKPAA TAAAAEAAPT PTEAEPAPAT EAVDAPAEKT AEAPEPEAPQ
     GGSAAALTEE KPAKAKGFGM AAGKKRPGGA SKAAPAAAAP APEAAPEPAP EAAPEPEQAP
     EPDAAQTDET PVEETPATEA PDASSNGSSA ARTVAEAGAS KAKGFGIAAG KKRPGHK
//
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