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Database: UniProt
Entry: Q3SGY7_THIDA
LinkDB: Q3SGY7_THIDA
Original site: Q3SGY7_THIDA 
ID   Q3SGY7_THIDA            Unreviewed;       763 AA.
AC   Q3SGY7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   SubName: Full=Elongator protein 3/MiaB/NifB {ECO:0000313|EMBL:AAZ98106.1};
GN   OrderedLocusNames=Tbd_2153 {ECO:0000313|EMBL:AAZ98106.1};
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415 {ECO:0000313|EMBL:AAZ98106.1, ECO:0000313|Proteomes:UP000008291};
RN   [1] {ECO:0000313|EMBL:AAZ98106.1, ECO:0000313|Proteomes:UP000008291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259 {ECO:0000313|EMBL:AAZ98106.1,
RC   ECO:0000313|Proteomes:UP000008291};
RX   PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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}.
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DR   EMBL; CP000116; AAZ98106.1; -; Genomic_DNA.
DR   RefSeq; WP_011312665.1; NC_007404.1.
DR   AlphaFoldDB; Q3SGY7; -.
DR   STRING; 292415.Tbd_2153; -.
DR   KEGG; tbd:Tbd_2153; -.
DR   eggNOG; COG1032; Bacteria.
DR   HOGENOM; CLU_018288_2_0_4; -.
DR   OrthoDB; 9803479at2; -.
DR   Proteomes; UP000008291; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
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; IPR019824; Leghaemoglobin_Fe_BS.
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; PS00208; PLANT_GLOBIN; 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}; Reference proteome {ECO:0000313|Proteomes:UP000008291};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01251}.
FT   DOMAIN          374..641
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          680..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         388
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         392
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         395
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   763 AA;  84248 MW;  1A058D1F65B98B74 CRC64;
     MTNALFSHRK HWAARFGTAP FLPMSRAEMA ALGWDACDVI LVAGDAYIDH PSFGMALVGR
     LLEAQGYRVG IISQPDWHSA DAFRVLGQPT LYFGVTAGNM DSMVNRYTSD RKIRSDDAYT
     ANAEPNKRPD RAVTVYAQRC REAFPGTPVI IGSIEASLRR IAHYDYWSDT VRRSVLPDSK
     ADLLIFGNAE RALLDISHRL AKGENIADIR DVRGTGFMVA RDWKPDEAWI EVLSTELDTP
     GAIDAHVDPY AMTPAGPTAQ TPEGTASIKT APVRIVPKAE RLAARQELRA RTVIRLPDYD
     QVRNNPALYA HASRVFHLES NPGNARALRQ GHGERDVWLN PPPIPLTTPE MDAVYDLPYA
     RAPHPSYGDA KIPAWEMIRF SINIMRGCFG GCTFCSITEH EGRIIQSRSE DSVIREIEAI
     RDKTPGFTGV ISDLGGPTAN MYRMACKSKQ IEQSCRRLSC VFPDICENMT TDHTPLIQMY
     RRARAVPGIK KIQISSGLRY DLAVRSPEYV KELVQHHVGG YLKIAPEHTE AGPLSKMMKP
     GMGAYERFKD MFEAASKAVG KKQYLIPYFI AAHPGTTDED MLNLALWLKK HDFRLDQVQT
     FLPTPMALAT AMYHTEKNPL KKVLGGKAET VPVVRQGRTR RLHKAFLRYH DPDNWPLLRQ
     ALKDMGREDL IGNGKKHLIP LYQPAGTGRQ PEGARSPCAA RAASGQAHGS KAGAGKPAAN
     KAAAVNTSAS KPSAGKPAPA SRGRPPQVPK HPLSQRRGGG KSR
//
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