ID   MAMA_CLOTT              Reviewed;         137 AA.
AC   Q05488;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Methylaspartate mutase S chain;
DE            EC=5.4.99.1;
DE   AltName: Full=Glutamate mutase subunit sigma;
GN   Name=mamA; Synonyms=mutS;
OS   Clostridium tetanomorphum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1553;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-33.
RC   STRAIN=NCIMB 11547;
RX   MEDLINE=93011908; PubMed=1397267; DOI=10.1016/0014-5793(92)81321-C;
RA   Marsh E.N.G., Holloway D.E.;
RT   "Cloning and sequencing of glutamate mutase component S from
RT   Clostridium tetanomorphum. Homologies with other cobalamin-dependent
RT   enzymes.";
RL   FEBS Lett. 310:167-170(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-24.
RC   STRAIN=ATCC 15920 / DSM 528 / H1;
RX   MEDLINE=93202282; PubMed=8454064; DOI=10.1016/0014-5793(93)80042-S;
RA   Brecht M., Kellermann J., Plueckthun A.;
RT   "Cloning and sequencing of glutamate mutase component E from
RT   Clostridium tetanomorphum.";
RL   FEBS Lett. 319:84-89(1993).
RN   [3]
RP   STRUCTURE BY NMR.
RC   STRAIN=ATCC 15920 / DSM 528 / H1;
RX   MEDLINE=98416697; PubMed=9739092; DOI=10.1016/S0969-2126(98)00103-8;
RA   Tollinger M., Konrat R., Hilbert B.H., Marsh E.N.G., Kraeutler B.;
RT   "How a protein prepares for B12 binding: structure and dynamics of the
RT   B12-binding subunit of glutamate mutase from Clostridium
RT   tetanomorphum.";
RL   Structure 6:1021-1033(1998).
CC   -!- CATALYTIC ACTIVITY: L-threo-3-methylaspartate = L-glutamate.
CC   -!- COFACTOR: 5'-deoxy-5'-adenosyl-adeninylcobamide (pseudo-coenzyme
CC       B12).
CC   -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via
CC       mesaconate pathway; acetate and pyruvate from L-glutamate: step
CC       1/4.
CC   -!- SUBUNIT: Heterotetramer of 2 E subunits and 2 S subunits. E exists
CC       as a homodimer and S as a monomer.
CC   -!- SIMILARITY: Contains 1 B12-binding domain.
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DR   EMBL; X70499; CAA49908.1; -; Genomic_DNA.
DR   EMBL; X68570; CAA48567.1; -; Genomic_DNA.
DR   PIR; S29502; S29502.
DR   PDB; 1BE1; NMR; -; A=1-137.
DR   PDB; 1FMF; NMR; -; A=1-137.
DR   PDB; 1ID8; NMR; -; A=1-137.
DR   PDBsum; 1BE1; -.
DR   PDBsum; 1FMF; -.
DR   PDBsum; 1ID8; -.
DR   BRENDA; 5.4.99.1; 2080.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050097; F:methylaspartate mutase activity; IEA:HAMAP.
DR   GO; GO:0019670; P:anaerobic glutamate catabolic process; IEA:HAMAP.
DR   HAMAP; MF_00526; -; 1.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR006394; Met_Asp_mutase.
DR   Gene3D; G3DSA:3.40.50.280; B12_bd; 1.
DR   Pfam; PF02310; B12-binding; 1.
DR   TIGRFAMs; TIGR01501; MthylAspMutase; 1.
DR   PROSITE; PS51332; B12_BINDING; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cobalamin; Cobalt; Direct protein sequencing; Isomerase;
KW   Metal-binding.
FT   CHAIN         1    137       Methylaspartate mutase S chain.
FT                                /FTId=PRO_0000216445.
FT   DOMAIN        3    137       B12-binding.
FT   METAL        16     16       Cobalt (cobalamin axial ligand).
FT   STRAND        5     11
FT   STRAND       25     28
FT   TURN         29     31
FT   STRAND       33     40
FT   HELIX        45     52
FT   STRAND       56     66
FT   HELIX        67     71
FT   HELIX        75     78
FT   STRAND       87     92
FT   STRAND       94     96
FT   HELIX       104    111
FT   STRAND      114    116
FT   TURN        123    128
FT   HELIX       129    132
SQ   SEQUENCE   137 AA;  14748 MW;  E71FE55BA8CE3DB3 CRC64;
     MEKKTIVLGV IGSDCHAVGN KILDHSFTNA GFNVVNIGVL SSQEDFINAA IETKADLICV
     SSLYGQGEID CKGLREKCDE AGLKGIKLFV GGNIVVGKQN WPDVEQRFKA MGFDRVYPPG
     TSPETTIADM KEVLGVE
//