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Database: UniProt
Entry: M0AN51_NATA1
LinkDB: M0AN51_NATA1
Original site: M0AN51_NATA1 
ID   M0AN51_NATA1            Unreviewed;       154 AA.
AC   M0AN51;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Cobalamin B12-binding domain-containing protein {ECO:0000313|EMBL:ELZ00146.1};
GN   ORFNames=C481_14159 {ECO:0000313|EMBL:ELZ00146.1};
OS   Natrialba asiatica (strain ATCC 700177 / DSM 12278 / JCM 9576 / FERM
OS   P-10747 / NBRC 102637 / 172P1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=29540 {ECO:0000313|EMBL:ELZ00146.1, ECO:0000313|Proteomes:UP000011554};
RN   [1] {ECO:0000313|EMBL:ELZ00146.1, ECO:0000313|Proteomes:UP000011554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12278 {ECO:0000313|EMBL:ELZ00146.1,
RC   ECO:0000313|Proteomes:UP000011554};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|ARBA:ARBA00001922};
CC   -!- SIMILARITY: Belongs to the methylamine corrinoid protein family.
CC       {ECO:0000256|ARBA:ARBA00010854}.
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:ELZ00146.1}.
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DR   EMBL; AOIO01000031; ELZ00146.1; -; Genomic_DNA.
DR   AlphaFoldDB; M0AN51; -.
DR   STRING; 29540.C481_14159; -.
DR   PATRIC; fig|29540.5.peg.2877; -.
DR   eggNOG; arCOG01710; Archaea.
DR   OMA; AHMTLFP; -.
DR   Proteomes; UP000011554; Unassembled WGS sequence.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   InterPro; IPR006159; Acid_CoA_mut_C.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR   PANTHER; PTHR48101:SF1; METHYLMALONYL-COA MUTASE, LARGE SUBUNIT; 1.
DR   PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000011554}.
FT   DOMAIN          25..154
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   154 AA;  16707 MW;  51CE1290DD1745B3 CRC64;
     MGMSSDQDED SQSQHHTQTA ERDRSIRCLV AKVGLDGHDR GAHVISRAFR DAGFEVIYSG
     LHKAPDEIVQ AAVQEDVDVL GISILSGAHD TLVPKIMDGL EEYGARDDTL VLVGGVIPDE
     DRPKLEDEGV AAIFGPGTSI EETIEFVREN APER
//
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