ID   A0A089XBT2_STRGA        Unreviewed;       675 AA.
AC   A0A089XBT2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE            EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN   Name=meaA {ECO:0000313|EMBL:AIS01388.1};
GN   ORFNames=SGLAU_27250 {ECO:0000313|EMBL:AIS01388.1};
OS   Streptomyces glaucescens.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1907 {ECO:0000313|EMBL:AIS01388.1, ECO:0000313|Proteomes:UP000029482};
RN   [1] {ECO:0000313|Proteomes:UP000029482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40922 / GLA O {ECO:0000313|Proteomes:UP000029482};
RX   PubMed=25499805; DOI=10.1016/j.jbiotec.2014.11.036;
RA   Ortseifen V., Winkler A., Albersmeier A., Wendler S., Puhler A.,
RA   Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of the actinobacterium Streptomyces glaucescens
RT   GLA.O (DSM 40922) consisting of a linear chromosome and one linear
RT   plasmid.";
RL   J. Biotechnol. 194:81-83(2015).
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; CP009438; AIS01388.1; -; Genomic_DNA.
DR   RefSeq; WP_043505094.1; NZ_CP009438.1.
DR   AlphaFoldDB; A0A089XBT2; -.
DR   STRING; 1907.SGLAU_27250; -.
DR   KEGG; sgu:SGLAU_27250; -.
DR   eggNOG; COG2185; Bacteria.
DR   HOGENOM; CLU_009523_4_0_11; -.
DR   OrthoDB; 9762378at2; -.
DR   Proteomes; UP000029482; 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:UP000029482}.
FT   DOMAIN          536..665
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51332"
SQ   SEQUENCE   675 AA;  73984 MW;  AE8BCAAD3366A7CC CRC64;
     MTERQKDRPW LMRTYAGHST AEASNELYRR NLAKGQTGLS VAFDLPTQTG YDPDHILARG
     EVGRVGVPVA HLGDMRRLFQ DIPLEQMNTS MTINATAMWL LALYQVVAEE QGADITRLQG
     TTQNDIVKEY LSRGTHVFPP GPSLRLTTDM IAYTVSHMPK WNPINICSYH LQEAGATPVQ
     EIAYAMSTAI AVLDAVRDSG QVPQERMGDV VARISFFVNA GVRFVEEMCK MRAFGRIWDK
     ITRERYGIEN PKQRRFRYGV QVNSLGLTEA QPENNVQRIV LEMLAVTLSK DARARAVQLP
     AWNEALGLPR PWDQQWSLRI QQVLAYESDL LEYDDIFEGS TVIEAKVGEL VAEALAEIER
     IQEMGGAMAA VESGYLKSQL VASHAERRAR IESGQEKIVG VNIFETTEPN PLTADLDTAI
     QTVDPAVEAR VVESLRNWRD TRYQPPFNHP RPCKALERLK EAAQGTGNLM EATLECARAG
     VTTGEWAGAL REVFGEFRAP TGVSSAPVAI AAEEGSTLAL VRRKVELTAQ EMGVGKLRFL
     VGKPGLDGHS NGAEQIAVRA RDAGFEVVYQ GIRLTPEQIV DAALAEDVHA VGLSILSGSH
     AQLVPDVLER LRVAGATDIP VIAGGIIPSG DAEQLRAAGV AAVFTPKDFD ITGIIGRIVD
     EIRTANKLDP LEVPA
//