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Database: UniProt
Entry: A0A1G3QU67_9SPIR
LinkDB: A0A1G3QU67_9SPIR
Original site: A0A1G3QU67_9SPIR 
ID   A0A1G3QU67_9SPIR        Unreviewed;       455 AA.
AC   A0A1G3QU67;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Radical SAM core domain-containing protein {ECO:0000259|PROSITE:PS51918};
GN   ORFNames=A2V99_00755 {ECO:0000313|EMBL:OHD70251.1};
OS   Spirochaetes bacterium RBG_16_67_19.
OC   Bacteria; Spirochaetota.
OX   NCBI_TaxID=1802196 {ECO:0000313|EMBL:OHD70251.1, ECO:0000313|Proteomes:UP000177018};
RN   [1] {ECO:0000313|EMBL:OHD70251.1, ECO:0000313|Proteomes:UP000177018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR603739-50};
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:OHD70251.1}.
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DR   EMBL; MIBK01000230; OHD70251.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G3QU67; -.
DR   STRING; 1802196.A2V99_00755; -.
DR   Proteomes; UP000177018; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR003739; Lys_aminomutase/Glu_NH3_mut.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR00238; KamA family radical SAM protein; 1.
DR   PANTHER; PTHR30538:SF1; L-LYSINE 2,3-AMINOMUTASE; 1.
DR   PANTHER; PTHR30538; LYSINE 2,3-AMINOMUTASE-RELATED; 1.
DR   Pfam; PF13353; Fer4_12; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01070; PLP-dependent; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603739-50};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          85..305
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   MOD_RES         310
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603739-50"
SQ   SEQUENCE   455 AA;  50373 MW;  A3BD4F8448AF7A15 CRC64;
     MTKPRDLPPG LELRPEERAF FRGHRREAPP FAVTRHLLGL LDPADPADPI RRQFLPTASE
     LSPGAGELED PLGEDRVQPV PNLLHRYPDR ALLLVTDRCA AYCRHCFRRR VSSGRRRAFL
     SPAELEQAAA YVDGHPEIRE LILSGGDPLL LSDARLRALF ARFRRERPEL ALRVHTRLPV
     VLPRRVTPAL VRLLAGFRPL RLVVQVNHPR ELDPACRQAL GLLAAAGLPL LAQSVLLAGV
     NDRPRTLAEL FAALSGAGVR PYYLFQPDLA RGTAHFRPDP ARGLRLYREA AALGPEAPRY
     MLDLPGGGGK VPVEPDLLGE REDGFYLLRR DGVVAARYPC YAGPMSTSGK KPKDFASVMR
     KTGKKLGKTL RGAAQATAKA AGKTAEVVAV RTRISAKQVR QKAEFLKMGE SFYRARKSGM
     SPEQILASMQ PQVTKLDTLQ QEIATLELRE KTLRN
//
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