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Database: UniProt
Entry: C0QAM2_DESAH
LinkDB: C0QAM2_DESAH
Original site: C0QAM2_DESAH 
ID   C0QAM2_DESAH            Unreviewed;       560 AA.
AC   C0QAM2;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Fe-S oxidoreductase family protein {ECO:0000313|EMBL:ACN16805.1};
GN   OrderedLocusNames=HRM2_37470 {ECO:0000313|EMBL:ACN16805.1};
OS   Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS   HRM2) (Desulfobacterium autotrophicum).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulforapulum.
OX   NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN16805.1, ECO:0000313|Proteomes:UP000000442};
RN   [1] {ECO:0000313|EMBL:ACN16805.1, ECO:0000313|Proteomes:UP000000442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC   {ECO:0000313|Proteomes:UP000000442};
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA   Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA   Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA   Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT   reducer oxidizing organic carbon completely to carbon dioxide.";
RL   Environ. Microbiol. 11:1038-1055(2009).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; CP001087; ACN16805.1; -; Genomic_DNA.
DR   RefSeq; WP_015905551.1; NC_012108.1.
DR   AlphaFoldDB; C0QAM2; -.
DR   STRING; 177437.HRM2_37470; -.
DR   KEGG; dat:HRM2_37470; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG1032; Bacteria.
DR   HOGENOM; CLU_021572_4_4_7; -.
DR   OrthoDB; 9804952at2; -.
DR   Proteomes; UP000000442; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd01335; Radical_SAM; 1.
DR   CDD; cd02068; radical_SAM_B12_BD; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 3.80.30.20; tm_1862 like domain; 1.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR034466; Methyltransferase_Class_B.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR43409; ANAEROBIC MAGNESIUM-PROTOPORPHYRIN IX MONOMETHYL ESTER CYCLASE-RELATED; 1.
DR   PANTHER; PTHR43409:SF17; MG-PROTOPORPHYRIN IX MONOMETHYL ESTER OXIDATIVE CYCLASE 66KD SUBUNIT; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR   SFLD; SFLDG01123; methyltransferase_(Class_B); 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00022485};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000442}.
FT   DOMAIN          8..143
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   DOMAIN          178..418
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   560 AA;  63434 MW;  B494047B90B0A98A CRC64;
     MTVLLVNPAC LDPRVTDGDA LLVPMGLFYI AALLNENRIP TQVVNLAVEE NPLDHLRSRV
     IAERPRIVGF SVLNANRFSA MEGAKVVKDV DPEILVVFGG PCATFLCDHL FSLCPELDYV
     VKGEGEITFL ELAEHLQRDE KHPAAMVQGL AHRGGLGKIV HTPERRPIED LDSLPIPGRY
     FDFQHVSLSR GCPGHCTFCG SPRFWPGARV RFHSPEWFVA QLSLLEKRGI NHFFVSDDTF
     TMDKTRVIKV CRIIIEQELP ITWVAISRVD FIDSEILLWM RRAGCTQISF GVESGSADIR
     KRLGKPMDRE RIVKAFALTV SYGIMPRAYF IYGSPGETDK TIRESLDLIM EIRPLSAIFY
     LLVLFPGTHL YQRLVDQGRL SDQLWSRKIE DLPWFEMDPD LDFDRVKTFG HALRKGFYSN
     LSDFAAGIEL VDEKSLYPLH ADFLSRLALT FSHGEYAQNP WVKKPMDTAQ LLFERALGYH
     PDHRAFLGLA MLFQKLRQFD SAIATATAGL RHFKSSRDLN ICMAVSLMNL GRFQDALGFL
     EPFKDNPEVK VYVDACIGRI
//
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