ID A0A099F1Z8_9RHOB Unreviewed; 652 AA.
AC A0A099F1Z8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Protein meaA {ECO:0000313|EMBL:KGJ04187.1};
GN ORFNames=IC63_12390 {ECO:0000313|EMBL:KGJ04187.1};
OS Paracoccus sphaerophysae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=690417 {ECO:0000313|EMBL:KGJ04187.1, ECO:0000313|Proteomes:UP000029917};
RN [1] {ECO:0000313|EMBL:KGJ04187.1, ECO:0000313|Proteomes:UP000029917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ04187.1,
RC ECO:0000313|Proteomes:UP000029917};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ04187.1, ECO:0000313|Proteomes:UP000029917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAMBI 3106 {ECO:0000313|EMBL:KGJ04187.1,
RC ECO:0000313|Proteomes:UP000029917};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) 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:KGJ04187.1}.
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DR EMBL; JRKS01000044; KGJ04187.1; -; Genomic_DNA.
DR RefSeq; WP_036720719.1; NZ_JRKS01000044.1.
DR AlphaFoldDB; A0A099F1Z8; -.
DR STRING; 690417.IC63_12390; -.
DR OrthoDB; 9762378at2; -.
DR Proteomes; UP000029917; 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:UP000029917}.
FT DOMAIN 519..648
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 652 AA; 71268 MW; F1154EBAD636776D CRC64;
MATKDKPWLF RTYAGHSTAA KSNELYRTNL AKGQTGLSVA FDLPTQTGYD SDHVLARGEV
GKVGVPVCHL GDMRALFDQI PLDQMNTSMT INATAPWLLS LYIAVAEEQG ADIAALQGTV
QNDIIKEYLS RGTYICPPKP SLRMITDVAA YTADHLPKWN PMNVCSYHLQ EAGATPEQEL
AYALATGIAV LDDLKGKVAP EDFPAMVGRI SFFVNAGIRF VTELCKMRAF TELWDEITRD
RYGIEDEKYR RFRYGVQVNS LGLTEQQPEN NVYRILIEML AVTLSKNARA RAVQLPAWNE
ALGLPRPWDQ QWSLRMQQIM AYETDLLEFG DLFDGNPAVA AKVEALKDGA RAELKLLDEM
GGAIAAIDYM KSQLVSSNAA RLNRIEDNET VVVGVNRWQQ GEPSPLTAGD GGIMVVDPAV
EADQIARLND WRASRDNPAV QAALAQLRED AAAGRNIMPA SIAAAKAGAT TGEWAGVMRQ
VHGEYRGPTG VSPSPSNRTE GLEPIREAVD AVSAKLGRRM KFVVGKPGLD GHSNGAEQIA
FRARDCGMDI TYDGIRLTPA EIVAAVRDEE AHVVGLSILS GSHLPLVEDV MTRMREEGLG
HVPVIVGGII PDEDARLLRA MGVTRVYTPK DFELNRIMMD LVALVDPQDK AA
//
