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Database: UniProt
Entry: Q72JU2_THET2
LinkDB: Q72JU2_THET2
Original site: Q72JU2_THET2 
ID   Q72JU2_THET2            Unreviewed;       142 AA.
AC   Q72JU2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Methylmalonyl-CoA mutase small subunit {ECO:0000313|EMBL:AAS81024.1};
DE            EC=5.4.99.2 {ECO:0000313|EMBL:AAS81024.1};
GN   OrderedLocusNames=TT_C0676 {ECO:0000313|EMBL:AAS81024.1};
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=262724 {ECO:0000313|EMBL:AAS81024.1, ECO:0000313|Proteomes:UP000000592};
RN   [1] {ECO:0000313|EMBL:AAS81024.1, ECO:0000313|Proteomes:UP000000592}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27
RC   {ECO:0000313|Proteomes:UP000000592};
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Overbeek R., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|ARBA:ARBA00001922};
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DR   EMBL; AE017221; AAS81024.1; -; Genomic_DNA.
DR   RefSeq; WP_011173118.1; NZ_CP133179.1.
DR   AlphaFoldDB; Q72JU2; -.
DR   GeneID; 3170009; -.
DR   KEGG; tth:TT_C0676; -.
DR   eggNOG; COG2185; Bacteria.
DR   HOGENOM; CLU_128233_0_0_0; -.
DR   OrthoDB; 9788468at2; -.
DR   Proteomes; UP000000592; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:AAS81024.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          7..135
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   142 AA;  15357 MW;  0C68C8FC2F400724 CRC64;
     MQGVDRRIRV LIAKPGLDGH DRGAKVVARA LRDAGMEVIY TGLRQTPEMI VSAAIQEDVD
     AIGLSILSGA HMHYFREVKR LLDEQGASDI LLFGGGIIPD EDVPKLKALG VAAVFGPGTS
     TQEIVDFLRR AVPERWKAQG LA
//
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