ID A0A0P7XL42_9RHOB Unreviewed; 717 AA.
AC A0A0P7XL42;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN Name=mut {ECO:0000313|EMBL:KPQ17347.1};
GN ORFNames=HLUCCO18_04785 {ECO:0000313|EMBL:KPQ17347.1};
OS Rhodobacteraceae bacterium HLUCCO18.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666917 {ECO:0000313|EMBL:KPQ17347.1, ECO:0000313|Proteomes:UP000050333};
RN [1] {ECO:0000313|EMBL:KPQ17347.1, ECO:0000313|Proteomes:UP000050333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCO18 {ECO:0000313|EMBL:KPQ17347.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-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:KPQ17347.1}.
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DR EMBL; LJSY01000008; KPQ17347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7XL42; -.
DR STRING; 1666917.HLUCCO18_04785; -.
DR PATRIC; fig|1666917.4.peg.30; -.
DR Proteomes; UP000050333; 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}.
FT DOMAIN 586..717
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 717 AA; 78352 MW; AFB6A89682EB0C05 CRC64;
MTENSRIKSD TTDAWRERAA KELKGRDPDS LVWETLEGIR VKPLYTEADT EGLPHMGTAP
GFEPFTRGVK ATMYAGRPWT IRQYAGFSTA EDSNNFYRKA LAAGQQGVSV AFDLATHRGY
DSDHPRVVGD VGKAGVAIDS VEDMKILFDG IPLDQVSVSM TMNGAVIPIL ANFIVTGEEQ
GHDRSVLSGT IQNDILKEFM VRNTYIYPPE PSMRIISDII GYTSENMPKF NSISISGYHM
QEAGANLVQE LAYTLADGRE YVRAAIDAGM DVDKFAGRLS FFFAIGMNFF MEIAKLRAAR
TLWHRIMTEF GAKSERSKML RTHCQTSGVS LQEQDPYNNV VRTAFEAMSA VLGGTQSLHT
NSFDEAIALP TEFSSRIARN TQLILQEETG VTKVVDPLAG SYYVESLTNE LIEKAWALIE
EVEEMGGMTK AVESGLPKLR IEESAARRQA MIDRGQEVIV GVNKYRKDHE DPIDILDIDN
VAVRESQIAR LERIRAARDE AACTAALAEV ERRAREGGNL LDAAVEAARA RASVGEISMA
MEKVFGRHRA EVKTLAGVYG SAYEGDEGFA QIQKDVDSFA EAEGRRPRML VVKMGQDGHD
RGAKVIATAF ADIGFDVDVG PLFQTPEEAA QDAIDNDVHV VGISSQAAGH KTLAPKLIEA
LKAEGAGDII VICGGVIPHQ DYEFLQKAGV KAIFGPGTNI PSAARDILEL IRAARAA
//
