ID A0A368VUL8_9ACTN Unreviewed; 746 AA.
AC A0A368VUL8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=DFQ14_10740 {ECO:0000313|EMBL:RCW43153.1};
OS Halopolyspora algeriensis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetes incertae sedis;
OC Halopolyspora.
OX NCBI_TaxID=1500506 {ECO:0000313|EMBL:RCW43153.1, ECO:0000313|Proteomes:UP000253495};
RN [1] {ECO:0000313|EMBL:RCW43153.1, ECO:0000313|Proteomes:UP000253495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8575 {ECO:0000313|EMBL:RCW43153.1,
RC ECO:0000313|Proteomes:UP000253495};
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 (JUL-2018) 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}.
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:RCW43153.1}.
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DR EMBL; QPJC01000007; RCW43153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368VUL8; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000253495; 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 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:UP000253495}.
FT DOMAIN 610..742
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 746 AA; 80361 MW; 0A3859962B213F0C CRC64;
MTQGDRVPSF ADIPLDDPVG SGGHEQWAGA VQAATGKEAD ALTWEAPEGI GIKPLYTSAD
TAELEFPRTY PGIAPYLRGP YSTMYVNQPW TVRQYAGFST ASESNAFYRR NLAAGQKGLS
VAFDLATHRG YDSDHPRVGG DVGMAGVAID SIYDMRQLFD GIPLDRMSVS MTMNGAVLPV
LALFIVAAEE QGVAPEQLAG TIQNDILKEF MVRNTYIYPP QPSMRIISDI FSYTSQKMPK
FNSISISGYH IQEAGATADL ELAYTLADGL DYIRAGRDAG LDIDSFAPRL SFFWGIGMHF
GMEVAKLRAA RLLWAKLVGR FSPQDPKSLS LRTHSQTSGW SLTAQDAFNN VARTCVEAMA
ATQGHTQSLH TNALDEALAL PTDFSARIAR NTQLVLQQES GTTRVIDPWG GSHYIERLTQ
DLAERAWAHI TEVEEAGGMA RAIDAGIPKL RIEEAAARTQ ARIDSGRQPL IGVNKYQPDA
DETDGAPEVR KVDNSAVRAE QLEKLQRLRQ ERDGEACAAA LDRLTAAAEA SVDGNRPGDL
EHNLLTLAVD AARAHATVGE ISDALEKVFG RHSGQIRTIS GVYTDEAGPS DNIERARALV
DEFAELEGRR PRILVAKMGQ DGHDRGQKVI ATAFADLGFD VDVGPLFQTP AEVAQQAAES
DVHLVGVSSL AAGHLTLVPA LREQLHAVGR DDIMITVGGV IPPADHEALH EAGAAAVFGP
GTVIAEAALG LLEQLRDQLD HDTGQS
//