ID A0A238KXG9_9RHOB Unreviewed; 657 AA.
AC A0A238KXG9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Methylmalonyl-CoA mutase {ECO:0000313|EMBL:SMX47330.1};
DE EC=5.4.99.2 {ECO:0000313|EMBL:SMX47330.1};
GN Name=scpA_2 {ECO:0000313|EMBL:SMX47330.1};
GN ORFNames=MAA8898_03631 {ECO:0000313|EMBL:SMX47330.1};
OS Maliponia aquimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Maliponia.
OX NCBI_TaxID=1673631 {ECO:0000313|EMBL:SMX47330.1, ECO:0000313|Proteomes:UP000207598};
RN [1] {ECO:0000313|EMBL:SMX47330.1, ECO:0000313|Proteomes:UP000207598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8898 {ECO:0000313|EMBL:SMX47330.1,
RC ECO:0000313|Proteomes:UP000207598};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-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}.
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DR EMBL; FXYF01000011; SMX47330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238KXG9; -.
DR Proteomes; UP000207598; 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:UniProtKB-EC.
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, ECO:0000313|EMBL:SMX47330.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000207598}.
FT DOMAIN 524..652
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 657 AA; 71926 MW; BFA1E21C87FFCE13 CRC64;
MTDTPMPPRD KPWLIRTYAG HSTAQASNAL YRSNLSKGQT GLSVAFDLPT QTGYDSDHVL
ARGEVGKVGV PVCHLGDMRA LFDQIPLDQM NTSMTINATA PWLLALYIAV AEEQGADVSQ
LQGTVQNDLI KEYLSRGTYI CPPKPSLKLI GDVAEYCYIN VPKWNPMNVC SYHLQEAGAT
PEQELAFALA TAIAVLDELK TRVPAEDFPT LCGRISFFVN AGIRFVTEMC KMRAFVDLWD
EILQERYGVE DPKVRRFRYG VQVNSLGLTE QQPENNVYRI LIEMLAVTLS KKARARAVQL
PAWNEALGLP RPWDQQWSMR MQQIMAFETD LLEFDDLFDG NPAVDAKVTE LKAGARAELA
NIDSMGGAVE AIEYMKGRLV DSNAERLNRI ERGETVVVGV NKFTHGEPSP LMDADGGIMT
VDPAVEQEQI DRLNAWRADR NEGMVKAALA DLRAAAVAGR NVMPASILCA RAGVTTGEWA
AQMRAVFGEY RGPTGVSRAV SNKTEGLDDL RAAVDAVSDR LGTRLRFLVG KPGLDGHSNG
AEQIAFRARD CGMEIDYEGI RLTPEQIVEA ARNGAHVVGL SILSGSHIPL VEELMDRMRA
EGLGHVPVIV GGIIPDEDAR RLTAMGVAQV YTPKDFELNA IMRDIVTLAD PASVAAQ
//
