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Database: UniProt
Entry: Q39VB8_GEOMG
LinkDB: Q39VB8_GEOMG
Original site: Q39VB8_GEOMG 
ID   Q39VB8_GEOMG            Unreviewed;       134 AA.
AC   Q39VB8;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=(R)-methylmalonyl-CoA mutase, adenosylcobamide-binding subunit {ECO:0000313|EMBL:ABB31806.1};
GN   OrderedLocusNames=Gmet_1574 {ECO:0000313|EMBL:ABB31806.1};
OS   Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB31806.1, ECO:0000313|Proteomes:UP000007073};
RN   [1] {ECO:0000313|EMBL:ABB31806.1, ECO:0000313|Proteomes:UP000007073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC   {ECO:0000313|Proteomes:UP000007073};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Geobacter metallireducens GS-15.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABB31806.1, ECO:0000313|Proteomes:UP000007073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC   {ECO:0000313|Proteomes:UP000007073};
RX   PubMed=19473543; DOI=10.1186/1471-2180-9-109;
RA   Aklujkar M., Krushkal J., DiBartolo G., Lapidus A., Land M.L., Lovley D.R.;
RT   "The genome sequence of Geobacter metallireducens: features of metabolism,
RT   physiology and regulation common and dissimilar to Geobacter
RT   sulfurreducens.";
RL   BMC Microbiol. 9:109-109(2009).
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|ARBA:ARBA00001922};
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DR   EMBL; CP000148; ABB31806.1; -; Genomic_DNA.
DR   RefSeq; WP_004511491.1; NC_007517.1.
DR   AlphaFoldDB; Q39VB8; -.
DR   STRING; 269799.Gmet_1574; -.
DR   KEGG; gme:Gmet_1574; -.
DR   eggNOG; COG2185; Bacteria.
DR   HOGENOM; CLU_128233_0_0_7; -.
DR   Proteomes; UP000007073; Chromosome.
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   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007073}.
FT   DOMAIN          5..133
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   134 AA;  14339 MW;  4705E353E04D0579 CRC64;
     MTERTLRILV GKPGLDGHDR GAKIIARAFR DAGFEVIYTG LHQTPEQIVS AAIQEDVDAV
     GLSILSGAHN ALLPRVCQLL KEKKADDIVV FGGGVIPDDD IPGLKRAGVS EVFTPGTSTE
     SIVQWVRENV APRA
//
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