ID D5EQ58_CORAD Unreviewed; 722 AA.
AC D5EQ58;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN OrderedLocusNames=Caka_0802 {ECO:0000313|EMBL:ADE53826.1};
OS Coraliomargarita akajimensis (strain DSM 45221 / IAM 15411 / JCM 23193 /
OS KCTC 12865 / 04OKA010-24).
OC Bacteria; Verrucomicrobiota; Opitutae; Puniceicoccales;
OC Coraliomargaritaceae; Coraliomargarita.
OX NCBI_TaxID=583355 {ECO:0000313|EMBL:ADE53826.1, ECO:0000313|Proteomes:UP000000925};
RN [1] {ECO:0000313|EMBL:ADE53826.1, ECO:0000313|Proteomes:UP000000925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45221 / IAM 15411 / JCM 23193 / KCTC 12865
RC {ECO:0000313|Proteomes:UP000000925};
RX PubMed=21304713; DOI=10.4056/sigs.952166;
RA Mavromatis K., Abt B., Brambilla E., Lapidus A., Copeland A., Deshpande S.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Han C., Detter J.C., Woyke T.,
RA Goodwin L., Pitluck S., Held B., Brettin T., Tapia R., Ivanova N.,
RA Mikhailova N., Pati A., Liolios K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Coraliomargarita akajimensis type strain
RT (04OKA010-24).";
RL Stand. Genomic Sci. 2:290-299(2010).
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; CP001998; ADE53826.1; -; Genomic_DNA.
DR RefSeq; WP_013042550.1; NC_014008.1.
DR AlphaFoldDB; D5EQ58; -.
DR STRING; 583355.Caka_0802; -.
DR KEGG; caa:Caka_0802; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_3_1_0; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000000925; 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 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, ECO:0000313|EMBL:ADE53826.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000925}.
FT DOMAIN 593..722
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 722 AA; 79473 MW; 96F84BE87719A632 CRC64;
MKPDFTNIAY EAPKPAATKE EWEAQVQAET GKSVKELVNE TMEQIDVDPL YGKDAYEGME
HLDYTAGIEP NLRGPYATMY AFRPWTVRQY AGFSTAEESN AFYRRNIAAG QQGLSVAFDL
ATHRGYDSDH PRVVGDVGKA GVAIDSIEDM KVLFDQIDLS KVSVSMTMNG AVLPVLAFYI
QAGIEQGCSL DQLAGTIQND ILKEFMVRNT YIYPPTPSMR IIGDIFEYTS QNMPKFNSIS
ISGYHMQEAG ATADLEIGYT LADGLEYLRT GTEAGLDIDA FAPRLSFFWA IGKNFFMEVA
KMRAARCLWA KLVKQFDPKN PKSLALRTHS QTSGWSLTEQ DPFNNVTRTA IEAMAAACGH
TQSLHTNALD EAIALPTDFS ARIARNTQLF IQEETGMCRF IDPWGGSYYV EALTQEIMHK
AWAHIEECEQ YGGMTKAIEE GIPKLRIEEA AARRQARIDS GKETIVGLNK YRLDKEDPLE
ILDIDNSAVR DSQVARLKEL KANRDNAAVT AALEAITKAC ETGEGNLLAL AVDAAAKRAS
LGEISDAVEK VVGRYKAKIR SISGVYSKEF GTTPAMDEIK TLISKFEEEE GRRPRIMIAK
MGQDGHDRGA KVVATGYADL GYDVDIGPLF QTPEETARQA VENDCHVVAM SSLAAGHKTL
LPELIGELKK LGREDIMVVC GGVIPAQDYD YLYENGAKAI FGPGTVIPES AQKILELLLE
DA
//
