ID E0NQK4_9BACT Unreviewed; 714 AA.
AC E0NQK4;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN Name=mutB {ECO:0000313|EMBL:EFM02578.1};
GN ORFNames=HMPREF0658_0455 {ECO:0000313|EMBL:EFM02578.1};
OS Hoylesella marshii DSM 16973 = JCM 13450.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=862515 {ECO:0000313|EMBL:EFM02578.1, ECO:0000313|Proteomes:UP000004394};
RN [1] {ECO:0000313|EMBL:EFM02578.1, ECO:0000313|Proteomes:UP000004394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16973 {ECO:0000313|EMBL:EFM02578.1,
RC ECO:0000313|Proteomes:UP000004394};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUL-2010) 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}.
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:EFM02578.1}.
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DR EMBL; AEEI01000020; EFM02578.1; -; Genomic_DNA.
DR RefSeq; WP_006948217.1; NZ_GL397214.1.
DR AlphaFoldDB; E0NQK4; -.
DR STRING; 862515.HMPREF0658_0455; -.
DR eggNOG; COG1884; Bacteria.
DR eggNOG; COG2185; Bacteria.
DR HOGENOM; CLU_009523_3_1_10; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000004394; 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.
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:EFM02578.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000004394}.
FT DOMAIN 586..714
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 714 AA; 78928 MW; 34091F537B553E00 CRC64;
MRKNFKNIDI FGGIKSVNGN EWQKKNGITA NWKTPEHIEV KPVYTKEDLD GMEHLDFTSG
LPPFLRGPYS MMYPFRPWTI RQYAGFSTAE ESNAFYRRNL ASGQKGLSVA FDLPTHRGYD
PDNERVVGDV GKAGVSICSV ENMKVLFDGI PLNKMSVSMT MNGAVLPIMA FYIVAGLEQG
AKLEEMAGTI QNDILKEFMV RNTYIYPPAF SMRIISDIFG YTSKYMPKFN SISISGYHMQ
EAGATADIEL AYTIADGLEY VRSGVAAGID IDAFAPRLSF FWGISMNHFM EIAKMRAARM
LWAKVIKQFN PKNDKSLALR THSQTSGWSL TEQDPFNNVG RTCIEAMAAA LGHTQSLHTN
ALDEAIALPT DFSARIARNT QIYVQNETKI CKEIDPWAGS YYVESLTNEL VHKAWEHIQE
VEKLGGMAKA IETGIPKMRI EESAARTQAR IDSGVQTILG TNKYRLEHED PIDILEVDNS
AVRRQQEEAL AQLKAHRDEQ KVKETLAALT ECVKTGEGNL LEKAVECAKV RCTLGEISDA
CEVIVGRYKA VIRTISGVYS SESKNDTDFD KACELTQEFA NKEGRRPRIF VAKMGQDGHD
RGAKVVATGY ADCGFDVDMG PLFQTPAEAA REAVENDVNI VGVSSLAAGH KTLVPQLIAE
LKKLGREDIM VIAGGVIPAQ DYDFLYKAGV AAIFGPGTSI AKSALTMMNI LLDK
//
