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Database: UniProt
Entry: H1G4K1_9GAMM
LinkDB: H1G4K1_9GAMM
Original site: H1G4K1_9GAMM 
ID   H1G4K1_9GAMM            Unreviewed;       728 AA.
AC   H1G4K1;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Radical SAM protein {ECO:0000313|EMBL:EHQ52738.1};
GN   ORFNames=ECTPHS_08608 {ECO:0000313|EMBL:EHQ52738.1};
OS   Ectothiorhodospira sp. PHS-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Ectothiorhodospira.
OX   NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ52738.1, ECO:0000313|Proteomes:UP000005314};
RN   [1] {ECO:0000313|EMBL:EHQ52738.1, ECO:0000313|Proteomes:UP000005314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ52738.1,
RC   ECO:0000313|Proteomes:UP000005314};
RA   Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V.,
RA   Hoeft S., Oremland R.S., Stolz J.;
RT   "ArxA, a new clade of arsenite oxidase within the DMSO family of molybdenum
RT   oxidoreductases.";
RL   Submitted (JAN-2012) 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:EHQ52738.1}.
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DR   EMBL; AGBG01000016; EHQ52738.1; -; Genomic_DNA.
DR   RefSeq; WP_008932305.1; NZ_AGBG01000016.1.
DR   AlphaFoldDB; H1G4K1; -.
DR   STRING; 519989.ECTPHS_08608; -.
DR   PATRIC; fig|519989.5.peg.1704; -.
DR   eggNOG; COG1032; Bacteria.
DR   OrthoDB; 9803479at2; -.
DR   Proteomes; UP000005314; Unassembled WGS sequence.
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:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
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};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01251}.
FT   DOMAIN          374..639
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          674..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..713
FT                   /note="Basic and acidic residues"
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   728 AA;  82360 MW;  48FD4544E5A4A702 CRC64;
     MTPSAVFRPL FSYRSYWAAR FGVAPFLPMS RHEMDQLGWD SCDVILVTGD AYIDHPSFGV
     AIIGRLLEAQ GFRVGVISQP DWRSSEPFQA LGRPNLFFGV TAGNMDSMVN RYTADRRLRS
     NDAYSPDDEG GRRPDRAVIV YSQRVREAYR DVPVIIGGIE ASLRRVAHYD YWSDKVRRSV
     LLDSRADLLI YGNGERALVE AAHRIARGEH PRDMKDLRGT AFLLDTPPGD WHVLDSTLVD
     RPGPVQRHRD PYCEEIPEQC GPGQAVAWGK AAGAQVIRVQ RRALTAHPRE RTVIRLPDCD
     TVQDDPVLYA HASRLIHLET NPGNARALVQ GHGDKDLWIN PPPIPLSTIE LDQLFDLPFA
     RAPHPAYRGA RIPAWEMIRF SVNIMRGCFG GCTFCSITEH EGRIIQSRSE DSIEREVDEI
     RDKVEGFTGI ISDLGGPTAN MYQLGCKDKA IEAHCRRLSC VHPRICRNLN TDHGPLIRLY
     RRIRQRPGVK KVLIASGLRY DLALESKEYV RELVTHHVGG YLKIAPEHTQ PGPLSRMMKP
     GIEVYERFRE LFERFSREAG KEQYLVPYFI AAHPGTTDED MLHLALWLKH NGFRLDQVQA
     FLPGPMALAT AMYHAERDPL KPVTRGSERV STAKGLRQRR LHKAFLRYHD PENWPLLREA
     LQRMGRADLI GNGKRHLVPR FQPAGTGTTG EGRRRPVQAA ERPASRRKSP RGPAPDRGAV
     AGRTRKRR
//
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