ID A0A0Q2UZ44_9RHOB Unreviewed; 655 AA.
AC A0A0Q2UZ44;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Protein meaA {ECO:0000313|EMBL:KQI69320.1};
GN ORFNames=AN189_05545 {ECO:0000313|EMBL:KQI69320.1};
OS Loktanella sp. 3ANDIMAR09.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=1225657 {ECO:0000313|EMBL:KQI69320.1, ECO:0000313|Proteomes:UP000051463};
RN [1] {ECO:0000313|EMBL:KQI69320.1, ECO:0000313|Proteomes:UP000051463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3ANDIMAR09 {ECO:0000313|EMBL:KQI69320.1,
RC ECO:0000313|Proteomes:UP000051463};
RA Mas-Llado M., Nogales B., Bosch R.;
RT "Draft genome sequence of Loktanella sp. 3ANDIMAR09.";
RL Submitted (SEP-2015) 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:KQI69320.1}.
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DR EMBL; LJAK01000003; KQI69320.1; -; Genomic_DNA.
DR RefSeq; WP_056033188.1; NZ_LJAK01000003.1.
DR AlphaFoldDB; A0A0Q2UZ44; -.
DR STRING; 1225657.AN189_05545; -.
DR PATRIC; fig|1225657.3.peg.1130; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000051463; 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 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:UP000051463}.
FT DOMAIN 521..650
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 655 AA; 71500 MW; 3B5491D5157F1725 CRC64;
MTETMKDRPW LFRTYAGHST AKASNALYRG NLAKGQTGLS VAFDLPTQTG YDSDHELSQG
EVGKVGVPVC HLGDMRALFD AIPLEQMNTS MTINATAPWL LALYIAVAEE QGADISALQG
TVQNDIIKEY LSRGTYICPP EASLRMITDV AAYTRAHLPK WNPMNICSYH LQEAGATPEE
ELSFALATAT AVLDDLRDKV SEADFPEMVG RISFFVNAGI RFVTELCKMR AFVELWDEIC
RDRYGVEDAK YRRFRYGVQV NSLGLTEQQP ENNVYRILIE MLAVTLSKNA RARAVQLPAW
NEALGLPRPW DQQWSLRMQQ ILAYETDLLE YEDLFDGNPA IERKVETLKQ GARAELAQID
AMGGAVKAIG YMKNRLVESN AARIRGIESG HTTVVGVNKW QAGEPSPLTA GEDAIMVADA
AAEADQLTRL AAWKQDRDPA AVEQAIAALR AAARDGSNMM PPSIQAAKAG VTTGEWAGIL
REVFGQFRGP TGVARAPSNQ TEGLDDLRAR VDAVSSTLGR RLKFMIGKPG LDGHSNGAEQ
IAARARDCGM DIAYEGIRLS PDALVAAAKQ DDPHVIGLSI LSGSHIPLIA TFMEKMRENG
LSHIPVVAGG IIPDEDAVRL LEMGIAKVYT PKDFELNRIM DDIVTLVNPT AVAAE
//
