ID Q1GPI6_SPHAL Unreviewed; 441 AA.
AC Q1GPI6;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=MiaB-like tRNA modifying enzyme {ECO:0000313|EMBL:ABF54436.1};
GN OrderedLocusNames=Sala_2731 {ECO:0000313|EMBL:ABF54436.1};
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655 {ECO:0000313|EMBL:ABF54436.1, ECO:0000313|Proteomes:UP000006578};
RN [1] {ECO:0000313|EMBL:ABF54436.1, ECO:0000313|Proteomes:UP000006578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256
RC {ECO:0000313|Proteomes:UP000006578};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP000356; ABF54436.1; -; Genomic_DNA.
DR RefSeq; WP_011543001.1; NC_008048.1.
DR AlphaFoldDB; Q1GPI6; -.
DR STRING; 317655.Sala_2731; -.
DR KEGG; sal:Sala_2731; -.
DR eggNOG; COG0621; Bacteria.
DR HOGENOM; CLU_018697_1_1_5; -.
DR OrthoDB; 9805215at2; -.
DR Proteomes; UP000006578; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035596; F:methylthiotransferase activity; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.40.50.12160; Methylthiotransferase, N-terminal domain; 1.
DR Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR005839; Methylthiotransferase.
DR InterPro; IPR020612; Methylthiotransferase_CS.
DR InterPro; IPR013848; Methylthiotransferase_N.
DR InterPro; IPR038135; Methylthiotransferase_N_sf.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR NCBIfam; TIGR00089; MiaB/RimO family radical SAM methylthiotransferase; 1.
DR PANTHER; PTHR11918; RADICAL SAM PROTEINS; 1.
DR PANTHER; PTHR11918:SF45; THREONYLCARBAMOYLADENOSINE TRNA METHYLTHIOTRANSFERASE; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF00919; UPF0004; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51449; MTTASE_N; 1.
DR PROSITE; PS01278; MTTASE_RADICAL; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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:UP000006578};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..124
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51449"
FT DOMAIN 150..376
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 107..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 47072 MW; 25740588D32A4EB3 CRC64;
MNAELADRVE VVNFGCRLNI AEGEAIRAAV KAAGARDMIV VNSCAVTDEA VRQARQAVRR
ALRERPDAEV VVTGCAAELE AGRFAAMGAR VVRNDVKGLI GSYGNTVSPR RREPISDGLE
MAPAGDGPPP SRGNKDFFSG VRPFTPALSG ADHARAFLGV QTGCSHSCTF CATVLARGAA
RSATVETVVD AARTALGRGQ REIILTGVDL ASYGDDSGTS LAALVEALLA LPVERLRLSS
LDPDRIDERL FALLTGESRV MPHVHLSLQA GDDMVLTRMK RRHRRADAVR LIERLKAARA
EIAIGADLIA GFPTEDEAMF ANSLALIDDC DVVFGHIFPY SPRAGTPAAR MPQVGRAIAR
ERAAMLREAN ARRRRDWLDT QVGRTAAMLV ERDGKTGHAE NFAALTLTAP AAPGTIIDVR
LIARDGDRMV ATPAEAKDIA A
//
