ID A0A161XDZ1_9EURY Unreviewed; 138 AA.
AC A0A161XDZ1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Methylmalonyl-CoA mutase {ECO:0000313|EMBL:KZN24171.1};
GN ORFNames=A4G99_06920 {ECO:0000313|EMBL:KZN24171.1};
OS Haladaptatus sp. R4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haladaptataceae; Haladaptatus.
OX NCBI_TaxID=1679489 {ECO:0000313|EMBL:KZN24171.1, ECO:0000313|Proteomes:UP000076599};
RN [1] {ECO:0000313|EMBL:KZN24171.1, ECO:0000313|Proteomes:UP000076599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R4 {ECO:0000313|EMBL:KZN24171.1,
RC ECO:0000313|Proteomes:UP000076599};
RA Mukhopadhyay S.K.;
RT "Genome sequence of halophilic archaea.";
RL Submitted (APR-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 methylamine corrinoid protein family.
CC {ECO:0000256|ARBA:ARBA00010854}.
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:KZN24171.1}.
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DR EMBL; LWHG01000021; KZN24171.1; -; Genomic_DNA.
DR RefSeq; WP_066143229.1; NZ_LWHG01000021.1.
DR AlphaFoldDB; A0A161XDZ1; -.
DR STRING; 1679489.A4G99_06920; -.
DR OrthoDB; 9041at2157; -.
DR Proteomes; UP000076599; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd02071; MM_CoA_mut_B12_BD; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR InterPro; IPR006159; Acid_CoA_mut_C.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR NCBIfam; TIGR00640; acid_CoA_mut_C; 1.
DR PANTHER; PTHR48101:SF1; METHYLMALONYL-COA MUTASE, LARGE SUBUNIT; 1.
DR PANTHER; PTHR48101; METHYLMALONYL-COA MUTASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02310; B12-binding; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 9..138
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 138 AA; 14868 MW; D0814CF40F62356B CRC64;
MSADQEQQSI RCLVAKVGLD GHDRGAHVIA RAFRDAGFEV IYSGLHNAPD EIVQAAVQED
VNVLGISILS GAHDTLVPKI VEGLKEYDAF DDTLILVGGV VPDDDKAELK ELGVAEVFGP
GTPMEETIEF VRENAPER
//
