ID F5SW62_9GAMM Unreviewed; 722 AA.
AC F5SW62;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Fe-S oxidoreductase {ECO:0000313|EMBL:EGL55503.1};
GN ORFNames=MAMP_02497 {ECO:0000313|EMBL:EGL55503.1};
OS Methylophaga aminisulfidivorans MP.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL55503.1, ECO:0000313|Proteomes:UP000003544};
RN [1] {ECO:0000313|EMBL:EGL55503.1, ECO:0000313|Proteomes:UP000003544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544};
RX PubMed=21685284; DOI=10.1128/JB.05403-11;
RA Han G.H., Kim W., Chun J., Kim S.W.;
RT "Draft genome sequence of Methylophaga aminisulfidivorans MP T.";
RL J. Bacteriol. 193:4265-4265(2011).
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:EGL55503.1}.
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DR EMBL; AFIG01000001; EGL55503.1; -; Genomic_DNA.
DR RefSeq; WP_007145389.1; NZ_AFIG01000001.1.
DR AlphaFoldDB; F5SW62; -.
DR STRING; 1026882.MAMP_02497; -.
DR eggNOG; COG1032; Bacteria.
DR OrthoDB; 9803479at2; -.
DR Proteomes; UP000003544; 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}; Reference proteome {ECO:0000313|Proteomes:UP000003544};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01251}.
FT DOMAIN 372..641
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 675..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 386
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 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 393
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 722 AA; 81009 MW; 0A87000D8626A25A CRC64;
MQSAPDLFSY RKFWAHRFGI APELPMTREE MDALGWDSCD IIIVTGDAYV DHPSFGMALI
GRLLESHGFR VGIISQPDWT GTDDFTKLGK PNLFFGVTGG NMDSMVNRYT SDRKIRSNDA
YTAGGSGGKR PDRSVVVYSQ RCQEAYKGVP VIIGGIEASL RRIAHYDYWS EKVRRSVIMD
SKADLLVYGN GERQVVEIAH RLAAGEPVSD LTDIRGTAYT KKHEQRPGWW EKDSTLVDTP
GKLNPPIDPY QMQTEESCAD EKAKTEQNKP AENTNVIKIH RVSPRNAERT VIRLPAYNAV
KDDPVTYAHT SRILHLETNP GNALALVQQH GNQDVWLNPP PIPLTTAEMD AVFDLPYSRV
PHSGYGKMTI PAYDMIRFSV NIMRGCFGGC TFCSITEHEG RIIQSRSEDS IIREVEAIRD
TTPGFTGVIS DLGGPTANMY RLACNDPQIE ASCRRLSCVF PGVCKNLNTD HTPLISLYKR
ARSLPGIKKI LIASGLRYDL AVLSPEYVKE LVTHHVGGYL KIAPEHTEEG PLQQMMKPGI
GTYDKFKQMF DKYSKEAGKE QYLIPYFIAA HPGTTDKDMM NLALWLKRNG FRADQVQAYL
PSPMSAAAAM YHSGKNTLHK VRRNGGDIEV PKGLKVRRLH KAFLRYHDPE NWPMLREALK
NMGRADLIGN GKKHLIPSWQ PAGTGENGEG RRVTRKAKNV QSFRTQHTRP GKTKVKAKRR
QR
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