ID   GMSS_HALSA              Reviewed;         149 AA.
AC   Q9HN21;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Glutamate mutase sigma subunit {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 {ECO:0000255|HAMAP-Rule:MF_00526};
DE   AltName: Full=Glutamate mutase small subunit {ECO:0000255|HAMAP-Rule:MF_00526};
DE   AltName: Full=Methylaspartate mutase {ECO:0000255|HAMAP-Rule:MF_00526};
GN   Name=glmS {ECO:0000255|HAMAP-Rule:MF_00526}; Synonyms=mamA;
GN   OrderedLocusNames=VNG_2286G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; AE004437; AAG20400.1; -; Genomic_DNA.
DR   PIR; D84379; D84379.
DR   RefSeq; WP_010903701.1; NC_002607.1.
DR   AlphaFoldDB; Q9HN21; -.
DR   SMR; Q9HN21; -.
DR   STRING; 64091.VNG_2286G; -.
DR   PaxDb; 64091-VNG_2286G; -.
DR   GeneID; 68694832; -.
DR   KEGG; hal:VNG_2286G; -.
DR   PATRIC; fig|64091.14.peg.1763; -.
DR   HOGENOM; CLU_136705_0_0_2; -.
DR   InParanoid; Q9HN21; -.
DR   OrthoDB; 225699at2157; -.
DR   PhylomeDB; Q9HN21; -.
DR   UniPathway; UPA00561; UER00617.
DR   Proteomes; UP000000554; Chromosome.
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..149
FT                   /note="Glutamate mutase sigma subunit"
FT                   /id="PRO_0000216449"
FT   DOMAIN          5..138
FT                   /note="B12-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
FT   BINDING         15..19
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
FT   BINDING         18
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         63..65
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
FT   BINDING         94..98
FT                   /ligand="adenosylcob(III)alamin"
FT                   /ligand_id="ChEBI:CHEBI:18408"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
SQ   SEQUENCE   149 AA;  15390 MW;  25A631D386055E29 CRC64;
     MSATDPTVVL GTIGSDAHAV GITLLDHALR EAGFTVHNLG AQTAKTEFAT AAADHDADAV
     LVSSLYGHAQ QDCAGLHDQL AAAGVDATTV VGGNLAVGQT DFETVKQRFE EMGFDRVFSA
     QTGFEAVVDA VKTELDVDER SPTTTTLGA
//