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Database: UniProt
Entry: A0A1E3XDP5_9BACT
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Original site: A0A1E3XDP5_9BACT 
ID   A0A1E3XDP5_9BACT        Unreviewed;       622 AA.
AC   A0A1E3XDP5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:ODS33718.1};
GN   ORFNames=SCARUB_01155 {ECO:0000313|EMBL:ODS33718.1};
OS   Candidatus Scalindua rubra.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Scalinduaceae; Scalindua.
OX   NCBI_TaxID=1872076 {ECO:0000313|EMBL:ODS33718.1, ECO:0000313|Proteomes:UP000094056};
RN   [1] {ECO:0000313|EMBL:ODS33718.1, ECO:0000313|Proteomes:UP000094056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSI-1 {ECO:0000313|EMBL:ODS33718.1};
RA   Speth D.R., Lagkouvardos I., Wang Y., Qian P.-Y., Dutilh B.E., Jetten M.S.;
RT   "Draft genome of Scalindua rubra, obtained from a brine-seawater interface
RT   in the Red Sea, sheds light on salt adaptation in anammox bacteria.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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:ODS33718.1}.
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DR   EMBL; MAYW01000021; ODS33718.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3XDP5; -.
DR   Proteomes; UP000094056; Unassembled WGS sequence.
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; 3.80.30.20; tm_1862 like domain; 1.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR034466; Methyltransferase_Class_B.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
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; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 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:UP000094056}.
FT   DOMAIN          6..143
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   DOMAIN          183..405
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   622 AA;  71406 MW;  BCED746214F54B0A CRC64;
     MSYFKNVCLL KAPQRIDIPY GLILSDITEV CYLAGMVKED VDSITIPVNT YASNPIHDFE
     RYLKSHPADM IGISSMTGAY TNALEYARIA RKHTLYVVLG GYHPTALPDE VLQSPYVDAV
     IRGEGEITFK ELVNEGPSEG VIGLSFKDNG NVIHNPDRDV IANLDVLPQP LREIRPKRFG
     NKGTDYLFDT VFTSRGCRIK CSFCSNDMVN KNWRCRSPEN VIEELKMIHT TKKRKILKIW
     DANVLTDVDR MERIIDLMFE NNLTNFKIWT ESRTTDIIRA ERIMKKLHDI GLRHVSLGIE
     SPNLETLKRI RKGTTPKTCE KAIEILNDYR IKVQGYFIIG HLNESIEDIK RYPEYAKTVG
     LKQAVFMVMT PYPGTQIFGE YKKENSINSY RWDMYNNFGT VVEPNKIDLK TLKKMLAYCN
     GKFYGIDSSS RQRTILGTVL EAIYRLINVA VIEKNDDRNS LNDLKNYMFE YLHALVGGNI
     KNAKFRDAKL LKYLGSKVIF RFFHSKGNSV DFKFTMNGSS ADLSITDSKK TDGYRCISFN
     LDDILNFEEH TPLKRIVALS SRYDIARANK ISKPIIFLKL AINKNFIATL YHLSIFITKT
     IIRSLFQNPR FTTEKSRNFT GN
//
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