ID M0MKP2_HALMO Unreviewed; 139 AA.
AC M0MKP2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Methylmalonyl-CoA mutase subunit B {ECO:0000313|EMBL:EMA45943.1};
GN ORFNames=C448_06835 {ECO:0000313|EMBL:EMA45943.1};
OS Halococcus morrhuae DSM 1307.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=931277 {ECO:0000313|EMBL:EMA45943.1, ECO:0000313|Proteomes:UP000011568};
RN [1] {ECO:0000313|EMBL:EMA45943.1, ECO:0000313|Proteomes:UP000011568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1307 {ECO:0000313|EMBL:EMA45943.1,
RC ECO:0000313|Proteomes:UP000011568};
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:EMA45943.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AOMC01000093; EMA45943.1; -; Genomic_DNA.
DR RefSeq; WP_004053084.1; NZ_AOMC01000093.1.
DR AlphaFoldDB; M0MKP2; -.
DR STRING; 931277.C448_06835; -.
DR PATRIC; fig|931277.6.peg.1329; -.
DR eggNOG; arCOG01710; Archaea.
DR OrthoDB; 9041at2157; -.
DR Proteomes; UP000011568; 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:InterPro.
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 Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011568}.
FT DOMAIN 9..138
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 139 AA; 14978 MW; F9BC7ADD74B50A3A CRC64;
MSAEQTQRPI RCLVAKVGLD GHDRGAHVIA RAFRDAGFEV VYSGLHRSPD EVVQAAVQED
VDVLGISILS GAHNTLVPKI LDGLDEYGAL DDTLVIVGGI VPDKDEDELR ERGVSAIFGP
GASMDDTIEF VRENAPKRE
//
