ID   GMSS2_HALMA             Reviewed;         148 AA.
AC   Q5V3F0;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Glutamate mutase sigma subunit 2 {ECO:0000255|HAMAP-Rule:MF_00526};
DE            EC=5.4.99.1 {ECO:0000255|HAMAP-Rule:MF_00526};
DE   AltName: Full=Glutamate mutase S chain 2 {ECO:0000255|HAMAP-Rule:MF_00526};
DE   AltName: Full=Glutamate mutase small subunit 2 {ECO:0000255|HAMAP-Rule:MF_00526};
DE   AltName: Full=Methylaspartate mutase 2 {ECO:0000255|HAMAP-Rule:MF_00526};
GN   Name=glmS2 {ECO:0000255|HAMAP-Rule:MF_00526}; Synonyms=mamA2;
GN   OrderedLocusNames=rrnAC0984;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
CC   -!- FUNCTION: Catalyzes the carbon skeleton rearrangement of L-glutamate to
CC       L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).
CC       {ECO:0000255|HAMAP-Rule:MF_00526}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3S)-3-methyl-L-aspartate = L-glutamate;
CC         Xref=Rhea:RHEA:12857, ChEBI:CHEBI:29985, ChEBI:CHEBI:58724;
CC         EC=5.4.99.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00526};
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00526};
CC   -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via mesaconate
CC       pathway; acetate and pyruvate from L-glutamate: step 1/4.
CC       {ECO:0000255|HAMAP-Rule:MF_00526}.
CC   -!- SUBUNIT: Heterotetramer composed of 2 epsilon subunits (GlmE) and 2
CC       sigma subunits (GlmS). GlmE exists as a homodimer and GlmS as a
CC       monomer. {ECO:0000255|HAMAP-Rule:MF_00526}.
CC   -!- SIMILARITY: Belongs to the methylaspartate mutase GlmS subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_00526}.
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DR   EMBL; AY596297; AAV45952.1; -; Genomic_DNA.
DR   RefSeq; WP_004961186.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V3F0; -.
DR   SMR; Q5V3F0; -.
DR   STRING; 272569.rrnAC0984; -.
DR   PaxDb; 272569-rrnAC0984; -.
DR   EnsemblBacteria; AAV45952; AAV45952; rrnAC0984.
DR   GeneID; 64822368; -.
DR   KEGG; hma:rrnAC0984; -.
DR   PATRIC; fig|272569.17.peg.1713; -.
DR   eggNOG; arCOG01710; Archaea.
DR   HOGENOM; CLU_136705_0_0_2; -.
DR   UniPathway; UPA00561; UER00617.
DR   Proteomes; UP000001169; Chromosome I.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050097; F:methylaspartate mutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019670; P:anaerobic glutamate catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019553; P:glutamate catabolic process via L-citramalate; IEA:UniProtKB-UniPathway.
DR   CDD; cd02072; Glm_B12_BD; 1.
DR   Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR   HAMAP; MF_00526; Me_Asp_mutase_S; 1.
DR   InterPro; IPR006158; Cobalamin-bd.
DR   InterPro; IPR036724; Cobalamin-bd_sf.
DR   InterPro; IPR006394; GlmS.
DR   NCBIfam; TIGR01501; MthylAspMutase; 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   Cobalamin; Cobalt; Isomerase; Metal-binding; Reference proteome.
FT   CHAIN           1..148
FT                   /note="Glutamate mutase sigma subunit 2"
FT                   /id="PRO_0000278196"
FT   DOMAIN          1..134
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
FT   REGION          129..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         11..15
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
FT   BINDING         14
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /ligand_part="Co"
FT                   /ligand_part_id="ChEBI:CHEBI:27638"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
FT   BINDING         59..61
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
FT   BINDING         90..94
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
SQ   SEQUENCE   148 AA;  15934 MW;  75FFF20F6795D515 CRC64;
     MRTVILGVIG SDAHVVGITI LERAFEAAGF NVVNLGVQSS QSEFIDAADE HDAEAILVSS
     LYGHAEQDCQ GFQQQINEAG LDVTTYIGGN LAVGQDSFEE TRETFKALGF DRVFNSETDP
     EEAIEALKAD LGHRSREEAS SEKVQLGS
//