GMSS1_HALMA
ID GMSS1_HALMA Reviewed; 151 AA.
AC Q5V467;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Glutamate mutase sigma subunit 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00526};
DE AltName: Full=Glutamate mutase small subunit 1 {ECO:0000255|HAMAP-Rule:MF_00526};
DE AltName: Full=Methylaspartate mutase 1 {ECO:0000255|HAMAP-Rule:MF_00526};
GN Name=glmS1 {ECO:0000255|HAMAP-Rule:MF_00526}; Synonyms=mamA1;
GN OrderedLocusNames=rrnAC0684;
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).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=21252347; DOI=10.1126/science.1196544;
RA Khomyakova M., Bukmez O., Thomas L.K., Erb T.J., Berg I.A.;
RT "A methylaspartate cycle in haloarchaea.";
RL Science 331:334-337(2011).
CC -!- FUNCTION: Catalyzes the carbon skeleton rearrangement of L-glutamate to
CC L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).
CC {ECO:0000305|PubMed:21252347}.
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; AAV45685.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5V467; -.
DR SMR; Q5V467; -.
DR STRING; 272569.rrnAC0684; -.
DR EnsemblBacteria; AAV45685; AAV45685; rrnAC0684.
DR KEGG; hma:rrnAC0684; -.
DR PATRIC; fig|272569.17.peg.1434; -.
DR eggNOG; arCOG01710; Archaea.
DR HOGENOM; CLU_136705_0_0_2; -.
DR OMA; GHGEMDC; -.
DR BioCyc; MetaCyc:MON-16253; -.
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 HAMAP; MF_00526; Me_Asp_mutase_S; 1.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR006394; GlmS.
DR Pfam; PF02310; B12-binding; 1.
DR SUPFAM; SSF52242; SSF52242; 1.
DR TIGRFAMs; TIGR01501; MthylAspMutase; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 3: Inferred from homology;
KW Cobalamin; Cobalt; Isomerase; Metal-binding; Reference proteome.
FT CHAIN 1..151
FT /note="Glutamate mutase sigma subunit 1"
FT /id="PRO_0000278195"
FT DOMAIN 7..140
FT /note="B12-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
FT BINDING 17..21
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
FT BINDING 20
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 65..67
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
FT BINDING 96..100
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00526"
SQ SEQUENCE 151 AA; 16306 MW; 3812223A02A9142A CRC64;
MTGKYMPRTV ILGVIGSDAH VVGITILEQA LSAAGFEVIN LGVQTAQDEF VSAAKSHDAE
AVLVSSLYGH ARQDCEGLHD ELDDAGLDVL TYVGGNLAVG QSDFEETQAT FRQMGFDRVF
DAETDPEEAI EMLREDLQLT TTEAEQIRVD G
