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Database: UniProt
Entry: A0A0A1I1U6_9PSED
LinkDB: A0A0A1I1U6_9PSED
Original site: A0A0A1I1U6_9PSED 
ID   A0A0A1I1U6_9PSED        Unreviewed;       771 AA.
AC   A0A0A1I1U6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Fe-S OXIDOREDUCTASE {ECO:0000313|EMBL:CDF96510.1};
DE            EC=1.8.-.- {ECO:0000313|EMBL:CDF96510.1};
GN   ORFNames=BN844_4969 {ECO:0000313|EMBL:CDF96510.1};
OS   Pseudomonas sp. SHC52.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=984195 {ECO:0000313|EMBL:CDF96510.1, ECO:0000313|Proteomes:UP000031550};
RN   [1] {ECO:0000313|EMBL:CDF96510.1, ECO:0000313|Proteomes:UP000031550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SHC52 {ECO:0000313|EMBL:CDF96510.1,
RC   ECO:0000313|Proteomes:UP000031550};
RA   Van der Voort M., Mendes R., Raaijmakers J.M.;
RT   "Genome mining of the rhizosphere bacterium Pseudomonas sp. SH-C52.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01251};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|HAMAP-Rule:MF_01251};
CC   -!- SIMILARITY: Belongs to the UPF0313 family. {ECO:0000256|HAMAP-
CC       Rule:MF_01251}.
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:CDF96510.1}.
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DR   EMBL; CBLV010000327; CDF96510.1; -; Genomic_DNA.
DR   RefSeq; WP_041024064.1; NZ_CBLV010000327.1.
DR   AlphaFoldDB; A0A0A1I1U6; -.
DR   OrthoDB; 9803479at2; -.
DR   Proteomes; UP000031550; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR   HAMAP; MF_01251; UPF0313; 1.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR020612; Methylthiotransferase_CS.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   InterPro; IPR022946; UPF0313.
DR   InterPro; IPR024560; UPF0313_C.
DR   InterPro; IPR013704; UPF0313_N.
DR   NCBIfam; TIGR03904; SAM_YgiQ; 1.
DR   PANTHER; PTHR32331; UPF0313 PROTEIN YGIQ; 1.
DR   PANTHER; PTHR32331:SF0; UPF0313 PROTEIN YGIQ; 1.
DR   Pfam; PF11842; DUF3362; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF08497; Radical_SAM_N; 1.
DR   SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SFLD; SFLDG01069; UPF0313; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS01278; MTTASE_RADICAL; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01251};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01251};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_01251};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01251}; Oxidoreductase {ECO:0000313|EMBL:CDF96510.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01251}.
FT   DOMAIN          376..654
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          686..771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        747..761
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         390
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01251"
FT   BINDING         394
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01251"
FT   BINDING         397
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01251"
SQ   SEQUENCE   771 AA;  86268 MW;  35CD2813E1EA03A4 CRC64;
     MQAAKPLFDY PKYWAECFGP APFLPMSREE MDQLGWDSCD IIIVTGDAYV DHPSFGMAII
     GRLLEAQGFR VGIIAQPNWQ SKDDFMKLGE PNLFFGVAAG NMDSMINRYT ADKKIRSDDA
     YTPGGLAGKR PDRASLVYSQ RCKEAYKHVP IVLGGIEASL RRIAHYDYWQ DRVRNSILID
     ASADILLYGN AERAIVEVAQ RLSYGHKIED ITDVRGTAFI RRDTPQGWYE VDSTRIDRPG
     KIDKIINPYV NTQDTQACAI EQEKGATVSS AVEDPSEAKV VQILASPKMT RDKTVIRLPS
     VEKVRNDAVL YAHANRVLHL ETNPGNARAL VQKHGEVDVW FNPPPIPMTT EEMDYVFGMP
     YARVPHPAYG KEKIPAYEMI RFSVNIMRGC FGGCTFCSIT EHEGRIIQNR SEESIIREIE
     EIRDKVPGFT GVISDLGGPT ANMYRIACKS PEIESACRKP SCVFPGICPN LNTDHSSLIQ
     LYRSARALPG VKKILIASGL RYDLAVESPE YVKELVTHHV GGYLKIAPEH TEEGPLNQMM
     KPGIGSYDRF KRMFEKYTKE AGKEQYLIPY FIAAHPGTTD EDMMNLALWL KGNGFRADQV
     QAFYPSPMAT ATAMYHSGKN PLRKVTYKSD GVTIVKSEEQ RRLHKAFLRY HDPKGWPMLR
     EALTRMGRAD LIGPGKHQLI PLHQPATDSY QSARRKNSTP AGSHKVGKDT TRILTQHTGL
     PPRASDGGNS WDKREQAKAA AFARNQQAAK ERKDAAKGKG PKPARKPVVP R
//
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