ID A0A0P1GP44_9RHOB Unreviewed; 661 AA.
AC A0A0P1GP44;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Methylmalonyl-CoA mutase {ECO:0000313|EMBL:CUH75927.1};
DE EC=5.4.99.2 {ECO:0000313|EMBL:CUH75927.1};
GN Name=scpA_1 {ECO:0000313|EMBL:CUH75927.1};
GN ORFNames=TRM7557_00625 {ECO:0000313|EMBL:CUH75927.1};
OS Tritonibacter multivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=928856 {ECO:0000313|EMBL:CUH75927.1, ECO:0000313|Proteomes:UP000052022};
RN [1] {ECO:0000313|EMBL:CUH75927.1, ECO:0000313|Proteomes:UP000052022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7557 {ECO:0000313|EMBL:CUH75927.1,
RC ECO:0000313|Proteomes:UP000052022};
RG Swine Surveillance;
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}.
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DR EMBL; CYSD01000012; CUH75927.1; -; Genomic_DNA.
DR RefSeq; WP_058288746.1; NZ_JAQIPA010000005.1.
DR AlphaFoldDB; A0A0P1GP44; -.
DR STRING; 928856.SAMN04488049_103157; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000052022; 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:CUH75927.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000052022}.
FT DOMAIN 529..658
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 661 AA; 72749 MW; 18247F6791627DF2 CRC64;
MTNAQSDQSQ VRQKDRPWLI RTYAGHSTAA KSNALYRANL AKGQTGLSVA FDLPTQTGYD
SDHVLSRGEV GKVGVPVCHL GDMRTLFDEI PLEQMNTSMT INATAPWLLS LYIAVAEEQG
ADISKLQGTV QNDLIKEYLS RGTYICPPQP SLKMIGDVAE YCYKHVPKWN PMNVCSYHLQ
EAGATPEQEL AFALATAQAV LDELRPRVSA EDFPRVVQRI SFFVNAGIRF VTEMCKMRAF
VDLWDEICQE RYGVEDPKAR RFRYGVQVNS LGLTEQQPEN NVYRILIEML AVTLSKKARA
RAVQLPAWNE ALGLPRPWDQ QWSMRMQQIL AYETDLLEYG DLFDGNPAVD AKVEALKEGA
RAELKTLESM GGAVASIEYM KSRLVDSNAE RINKIESNET VVVGVNKWTE GEPSPLQTED
GGIMVVDPAV EQEQIARLNS WRSTRDAKAV AEALADLREA ARTGANIVPP SVKAAKAGVT
TGEWAEEMRK VHGTYRGPTG VSASQSNMTE GLDDLREAVN AVSDQLGRRL KFVVGKPGLD
GHSNGAEQIA YRARDCGMDI TYDGIRLTPQ ELADSAEKDG AHVIGLSILS GSHLPLVKDT
LAQLEDAGLG HVPVVVGGII PDDDAVKLRE MGVSRVYTPK NFELNAIMHD IVNLAKPDQD
R
//
