ID A0A0T5ZSP8_9BACT Unreviewed; 675 AA.
AC A0A0T5ZSP8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Methylmalonyl-CoA mutase {ECO:0000313|EMBL:KRT65786.1};
GN Name=meaA {ECO:0000313|EMBL:KRT65786.1};
GN ORFNames=XU11_C0019G0007 {ECO:0000313|EMBL:KRT65786.1};
OS Candidatus Dadabacteria bacterium CSP1-2.
OC Bacteria; Thermodesulfobacteriota; Candidatus Dadabacteria.
OX NCBI_TaxID=1640508 {ECO:0000313|EMBL:KRT65786.1, ECO:0000313|Proteomes:UP000051780};
RN [1] {ECO:0000313|EMBL:KRT65786.1, ECO:0000313|Proteomes:UP000051780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-2 {ECO:0000313|EMBL:KRT65786.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000256|ARBA:ARBA00008465}.
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:KRT65786.1}.
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; LDXN01000019; KRT65786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZSP8; -.
DR STRING; 1640508.XU11_C0019G0007; -.
DR PATRIC; fig|1640508.3.peg.1226; -.
DR Proteomes; UP000051780; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:InterPro.
DR CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 1.
DR InterPro; IPR006159; Acid_CoA_mut_C.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR InterPro; IPR006098; MMCoA_mutase_a_cat.
DR NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR NCBIfam; TIGR00641; acid_CoA_mut_N; 1.
DR PANTHER; PTHR48101:SF3; COENZYME B12-DEPENDENT MUTASE; 1.
DR PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF01642; MM_CoA_mutase; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 542..671
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 675 AA; 75407 MW; 3E7BE4C06A560D7E CRC64;
MSSKPEEKPK KQSFDKAAQG VKDNPWIMRT YAGHTTAKAS NELFRKNLAK GQTGLSVAFD
LPTQTGYDSV HPLAEGEVGK VGVPIGHIED MDALFDKIPI EKMNTSMTIN ATAAWLLSLY
IALAERRGVD ISQLEGTTQN DILKEYLSRG TYIFPPKPSM RLISDTITFT FSKVPKWNPI
NICSYHLQEA GATPVQEIAF TLANAIAVLD TVRESGQIPK DRFPQVVGRI SFFVNAGIRF
IEEMCKMRAF TEMWDELTLK RYGVGDEKYR RFRYGVQVNS LGLTAQQPEN NIARILLEML
AVTLSKNARA RAIQLPAWNE ALGLPRPWDQ QWSLRFQQIL AYETDLLEYP DIFDGSPVIE
RKGRDLKKEA WKEIERIEEI GGALSAIEKG YMKMALVASH AGRVRAIEKG EIQIVGVNCF
TETEQSPLVQ SVEESIQKVD PKVVRQQLER LKAFKIKRNE KAVKEALREL SEAAKSDINI
MPASIHCAHA GVTTGEWADT FRRVFGEYRA PTGTSITLRE DTNEIRSVRN EVKSLREKLG
RPPKVLIGKP GLDGHSNGAE QIAVRARDVG MEVLYQGIRL TPEEIVSTAE QENVDIIGLS
ILSGSHDTII PKIMNLLNEK GLGDIPVIAG GIIPDDDAKL LIATGIKRVY TPKDYSLNRI
MHDIVEIIKE SKDNV
//
