ID A0A0N7F555_9PSEU Unreviewed; 664 AA.
AC A0A0N7F555;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=AOZ06_46245 {ECO:0000313|EMBL:ALG13287.1};
OS Kibdelosporangium phytohabitans.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kibdelosporangium.
OX NCBI_TaxID=860235 {ECO:0000313|EMBL:ALG13287.1, ECO:0000313|Proteomes:UP000063699};
RN [1] {ECO:0000313|EMBL:ALG13287.1, ECO:0000313|Proteomes:UP000063699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLBMP1111 {ECO:0000313|EMBL:ALG13287.1,
RC ECO:0000313|Proteomes:UP000063699};
RA Qin S., Xing K.;
RT "Genome sequencing of Kibdelosporangium phytohabitans.";
RL Submitted (JUL-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 -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
CC -!- SIMILARITY: Belongs to the methylmalonyl-CoA mutase family.
CC {ECO:0000256|ARBA:ARBA00008465}.
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DR EMBL; CP012752; ALG13287.1; -; Genomic_DNA.
DR RefSeq; WP_054295176.1; NZ_JADBEI010000001.1.
DR AlphaFoldDB; A0A0N7F555; -.
DR STRING; 860235.AOZ06_46245; -.
DR KEGG; kphy:AOZ06_46245; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000063699; Chromosome.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000063699}.
FT DOMAIN 530..659
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 664 AA; 72320 MW; 8D17BD548B0A4226 CRC64;
MPYPTDRERD RPWVMRTYAG HSSATASNAL YRRNLAKGQT GLSVAFDLPT QTGYDPDHEL
SRGEVGKVGV PISHVGDMRQ LFDGIPLAEA NTSMTINSTA MWLLAMYTTV AEEQGADIGK
LMGTTQNDII KEYLSRGTYV FPPGPSLRLI TDMVAWTVTN VPKWNPINIC SYHLQEVGAN
PVQELAYSMC TAIAVLDAVR DSGQVPQEEF GSVVARMSFF VNAGVRFVEE MCKMRAFAAL
WDEITLERYG VQNPKHRRFR YGVQVNSLGL TEAQPENNVQ RIVLEMLAVS LSRSARARAI
QLPAWNEALG LPRPWDQQWA LRMQQVLAYE TDLLEYEDIF DGSPVIEAKV DEILRGAREE
IDRVQAMGGA VAAVESGYMK TQLVGSLASR RVRIENGEEV IVGVNKFDTT EPSPLQAEGA
KAIEQLDPAV EKDAVAAIQR WRAGRDQTQV EESLEALRAA AKTDVNLVTA TLTCVKAGVT
TGEWAGALRE VFGEYRAPTG VAGVSTGEAG VELARVRDRV QRTSTELGER LRMLVGKPGL
DGHSNGAEQV AVRARDVGFE VVYQGIRLTP DQIVAAAVQE GVHVVGLSVL SGSHLEVVPA
VVEGLRAAGA DDIPVVVGGI VPPDDAKALL DRGIARVFTP KDYELTEIMA GIVDLVRETR
GLIG
//
