(data stored in SCRATCH zone)

SWISSPROT: B8IT27_METNO

ID   B8IT27_METNO            Unreviewed;       690 AA.
AC   B8IT27;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   SubName: Full=Methylmalonyl-CoA mutase, large subunit {ECO:0000313|EMBL:ACL55089.1};
DE            EC=5.4.99.2 {ECO:0000313|EMBL:ACL55089.1};
GN   OrderedLocusNames=Mnod_0038 {ECO:0000313|EMBL:ACL55089.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55089.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55089.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001349; ACL55089.1; -; Genomic_DNA.
DR   ProteinModelPortal; B8IT27; -.
DR   STRING; 460265.Mnod_0038; -.
DR   EnsemblBacteria; ACL55089; ACL55089; Mnod_0038.
DR   KEGG; mno:Mnod_0038; -.
DR   eggNOG; ENOG4105RFZ; Bacteria.
DR   eggNOG; COG1884; LUCA.
DR   eggNOG; COG2185; LUCA.
DR   HOGENOM; HOG000003917; -.
DR   KO; K14447; -.
DR   OMA; QMNTSMT; -.
DR   OrthoDB; POG091H0B8X; -.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004494; F:methylmalonyl-CoA mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.240; -; 1.
DR   InterPro; IPR006159; Acid_CoA_mut_C.
DR   InterPro; IPR016176; Cbl-dep_enz_cat.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR006099; MeMalonylCoA_mutase_a/b_cat.
DR   InterPro; IPR006098; MMCoA_mutase_a_cat.
DR   Pfam; PF02310; B12-binding; 1.
DR   Pfam; PF01642; MM_CoA_mutase; 1.
DR   SUPFAM; SSF51703; SSF51703; 1.
DR   SUPFAM; SSF52242; SSF52242; 1.
DR   TIGRFAMs; TIGR00640; acid_CoA_mut_C; 1.
DR   TIGRFAMs; TIGR00641; acid_CoA_mut_N; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
PE   4: Predicted;
DR   PRODOM; B8IT27.
DR   SWISS-2DPAGE; B8IT27.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Isomerase {ECO:0000313|EMBL:ACL55089.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207}.
FT   DOMAIN      544    673       B12-binding. {ECO:0000259|PROSITE:
FT                                PS51332}.
SQ   SEQUENCE   690 AA;  75402 MW;  C8BCF39109306C9C CRC64;
     MPPPRGLRNT RDEGAMGDQA MGTAQRDKPW IIRTYAGHST AAESNALYRR NLAKGQTGLS
     VAFDLPTQTG YDPDHELARG EVGKVGVSIA HLGDMRTLFK DIPLAQMNTS MTINATAPWL
     LSLYLAVAEE QGAPISVLQG TTQNDIIKEY LSRGTYVFPP APSLRLTKDV ILFTTKQVPK
     WNPMNVCSYH LQEAGATPVQ ELSYALAIAI AVLDTVRADP DFDEASFSEV VGRISFFVNA
     GLRFITEICK MRAFCDLWDE ITRDRYGITD PKKRIFRYGV QVNSLGLTEQ QPENNVHRIL
     IEMLAVTLSK RARARAVQLP AWNEALGLPR PWDQQWSMRM QQILAYETDL LEFDDIFDGS
     KVIDAKVEAL KAETRSELER IGALGGAVAA VETGALKRAL VESNARRIAA IERGEQVVVG
     VNRFETGEPS PLTAGDGAIF TVSETVEMEA QQRIRAWRAE RDAKAVARAL DDLEAAARSG
     ANIMPVSIAC AKAGVTTGEW GERLREVFGE YRAPTGVTPE TTTSGAAEEA RLLIADLGER
     LGETPKLVVG KPGLDGHSNG AEQIALRARD VGFDVTYDGI RQTPDEIVAK ARERGAHVIG
     LSILSGSHVP LVREVKARLR REGLDHVPVV VGGIISPEDE LVLKNMGVAA VYTPKDYAMD
     TIMVGLAKVV EKALARREAD SALPNREQVF
//

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