ID A0A2N0I3D7_9SPHN Unreviewed; 711 AA.
AC A0A2N0I3D7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=B0I00_0897 {ECO:0000313|EMBL:PKB25691.1};
OS Novosphingobium kunmingense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1211806 {ECO:0000313|EMBL:PKB25691.1, ECO:0000313|Proteomes:UP000232587};
RN [1] {ECO:0000313|EMBL:PKB25691.1, ECO:0000313|Proteomes:UP000232587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12274 {ECO:0000313|EMBL:PKB25691.1,
RC ECO:0000313|Proteomes:UP000232587};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (NOV-2017) 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:PKB25691.1}.
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; PHUF01000002; PKB25691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0I3D7; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000232587; 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 CDD; cd03679; MM_CoA_mutase_alpha_like; 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:SF4; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL; 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.
DR PROSITE; PS00544; METMALONYL_COA_MUTASE; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000232587}.
FT DOMAIN 572..704
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 711 AA; 76698 MW; 216B88ACB4B370BD CRC64;
MAGIEDWQAA ATKEVKGKDL TWNTPEGIAV KPLYTAEDVT ADPGLPGFAP FTRGVRASMY
AGRPWTIRQY AGFSTAEESN AFYRRNLAAG QKGLSVAFDL ATHRGYDSDH PRVVGDVGKA
GVAIDSVDDM KILFDGIPLD QMSVSMTMNG AVIPILAFFI VAGEEQGVDR KLLDGTIQND
ILKEFMVRNT YIYPPEPSMR IISDIFGYTS REMPKFNSIS ISGYHMQEAG ATQVQELAFT
IADGMEYVKY GVASGLDIDK FAGRLSFFFA IGMNFFMEVA KLRAARVLWH RVMTRLGAQD
ERSKMLRTHC QTSGVSLQEQ DPYNNVIRTT IEAMAAMLGG TQSLHTNALD EAIALPTDFS
ARIARNTQIV IQEETGMTKV VDPLGGSYYI EALTQELVDQ AWAIIERVEA EGGMAKAVAA
GWPKAMIEEA AAGRQARVDK GEDVIVGVNK YRLASEDQLE TLEVDNHVVR EGQIARLKAT
RAARDEGKCQ AALAALTEGA RGQGNLLELA VEAARHRATL GEISDAMEAV FGRYGTQPTP
VKGIYGGAYA GDSRYQQVLD GVEAVERRLG RKPRILIAKM GQDGHDRGAN VIASAFSDMG
FDVTSGPLFQ TPEETVVLAL ESGVDAVGAS SLAAGHKTLI PELIQRLKEA GRGDIKVVAG
GVIPPQDYDF LRDAGVQGIY GPGSNVVECA ADMLRLLGHN MPPAGGEAEA A
//
