ID A0A1B7ZFU6_9FLAO Unreviewed; 724 AA.
AC A0A1B7ZFU6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=methylmalonyl-CoA mutase {ECO:0000256|ARBA:ARBA00012398};
DE EC=5.4.99.2 {ECO:0000256|ARBA:ARBA00012398};
GN ORFNames=A9200_01340 {ECO:0000313|EMBL:OBR42404.1};
OS Maribacter hydrothermalis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=1836467 {ECO:0000313|EMBL:OBR42404.1, ECO:0000313|Proteomes:UP000092164};
RN [1] {ECO:0000313|Proteomes:UP000092164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T28 {ECO:0000313|Proteomes:UP000092164};
RA Zhan P.;
RL Submitted (JUN-2016) 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:OBR42404.1}.
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DR EMBL; LZFP01000001; OBR42404.1; -; Genomic_DNA.
DR RefSeq; WP_068481840.1; NZ_LZFP01000001.1.
DR AlphaFoldDB; A0A1B7ZFU6; -.
DR STRING; 1836467.BTR34_09710; -.
DR KEGG; mart:BTR34_09710; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000092164; 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:InterPro.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000092164}.
FT DOMAIN 595..724
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 724 AA; 80059 MW; BBE23E6C8B04142F CRC64;
MSRKDLSHIT LSTDGDSKII GVTERSRSEA YENAEKIILK SAFSKEDIKE IEHLNFAAGI
PPFLRGPYST MYVRRPWTIR QYAGFSTAEE SNAFYRRNLK GGQKGLSVAF DLPTHRGYDS
DHERVIGDVG KAGVAIDSVE DMKILFDGIP LDKMSVSMTM NGAVLPIMAF YIVAAEEQGV
DKALLAGTIQ NDILKEFMVR NTYIYPPKPS MQLVADIFEY TSQLMPKFNS ISISGYHMHE
AGASADIELA YTLADGLEYI KTGLKAGLKI DDFAPRLSFF WGIGMNHFME IAKMRAARML
WAKLVKQFNP KSEKSLALRT HCQTSGWSLT EQDPFNNVAR TTIEATAAIL GGTQSLHTNA
LDEAIALPTD FSARIARETQ IFLQEETKIT KTVDPWAGSY YVEYLTDELV KKAWVLMEEV
EELGGMTKAI EAGIPKLRIE QAAARKQARI DSVNDVIVGV NKFQLKEEDD LQILEVDNQE
VRRQQLVRLA SIKNTRDENA VNNALIELKE AAKLKMADND QNLPADKNLL ALAVNAARVR
ATLGEISAAL ESVFGRHKAV INSFSGVYSK EIKDDKSFLK AKVLCDQFAE QDGRRPRIMI
AKMGQDGHDR GAKVVATGYA DLGFDVDIGP LFQTPEESAK QAVENDVHIL GVSSLAAGHK
TLVPAVIKEL KKYGREDIMV IVGGVIPKQD YQFLYDAGAT AVFGPGTKIS DAAIQLLAIL
IEKE
//
