ID A0A346PQ64_9EURY Unreviewed; 473 AA.
AC A0A346PQ64; A0A346PFL5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 02-APR-2025, entry version 23.
DE RecName: Full=Glutamate mutase epsilon subunit {ECO:0000256|HAMAP-Rule:MF_01923};
DE EC=5.4.99.1 {ECO:0000256|HAMAP-Rule:MF_01923};
DE AltName: Full=Glutamate mutase E chain {ECO:0000256|HAMAP-Rule:MF_01923};
DE AltName: Full=Glutamate mutase large subunit {ECO:0000256|HAMAP-Rule:MF_01923};
DE AltName: Full=Methylaspartate mutase {ECO:0000256|HAMAP-Rule:MF_01923};
GN Name=glmE {ECO:0000256|HAMAP-Rule:MF_01923};
GN ORFNames=AArc1_1991 {ECO:0000313|EMBL:AXR78310.1}, AArcMg_1648
GN {ECO:0000313|EMBL:AXR81659.1};
OS Natrarchaeobaculum sulfurireducens.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Halobacteria; Halobacteriales; Natrialbaceae; Natrarchaeobaculum.
OX NCBI_TaxID=2044521 {ECO:0000313|EMBL:AXR81659.1, ECO:0000313|Proteomes:UP000258613};
RN [1] {ECO:0000313|Proteomes:UP000258707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AArc1 {ECO:0000313|Proteomes:UP000258707};
RA Sorokin D.Y., Kublanov I.V., Roman P., Sinninghe Damste J.S.,
RA Golyshin P.N., Rojo D., Ciordia S., Mena Md.C., Ferrer M., Messina E.,
RA Smedile F., La Spada G., La Cono V., Yakimov M.M.;
RT "Phenotypic and genomic properties of facultatively anaerobic sulfur-
RT reducing natronoarchaea from hypersaline soda lakes.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000258613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AArc-Mg {ECO:0000313|Proteomes:UP000258613};
RA Sorokin D.Y., Kublanov I.V., Roman P., Sinninghe Damste J.S.,
RA Golyshin P.N., Rojo D., Ciordia S., Mena M.D.C., Ferrer M., Messina E.,
RA Smedile F., La Spada G., La Cono V., Yakimov M.M.;
RT "Phenotypic and genomic properties of facultatively anaerobic sulfur-
RT reducing natronoarchaea from hypersaline soda lakes.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AXR81659.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AArc-Mg {ECO:0000313|EMBL:AXR81659.1}, and AArc1
RC {ECO:0000313|EMBL:AXR78310.1};
RX PubMed=31166158;
RA Sorokin D.Y., Yakimov M., Messina E., Merkel A.Y., Bale N.J.,
RA Sinninghe Damste J.S.;
RT "Natronolimnobius sulfurireducens sp. nov. and Halalkaliarchaeum
RT desulfuricum gen. nov., sp. nov., the first sulfur-respiring alkaliphilic
RT haloarchaea from hypersaline alkaline lakes.";
RL Int. J. Syst. Evol. Microbiol. 69:2662-2673(2019).
CC -!- FUNCTION: Catalyzes the carbon skeleton rearrangement of L-glutamate to
CC L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).
CC {ECO:0000256|HAMAP-Rule:MF_01923}.
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:0000256|HAMAP-Rule:MF_01923};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01923};
CC -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via mesaconate
CC pathway; acetate and pyruvate from L-glutamate: step 1/4.
CC {ECO:0000256|HAMAP-Rule:MF_01923}.
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:0000256|HAMAP-Rule:MF_01923}.
CC -!- SIMILARITY: Belongs to the methylaspartate mutase GlmE subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01923}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01923}.
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DR EMBL; CP024047; AXR78310.1; -; Genomic_DNA.
DR EMBL; CP027033; AXR81659.1; -; Genomic_DNA.
DR RefSeq; WP_117364398.1; NZ_CP024047.1.
DR AlphaFoldDB; A0A346PQ64; -.
DR GeneID; 37642130; -.
DR KEGG; nag:AArcMg_1648; -.
DR KEGG; nan:AArc1_1991; -.
DR OrthoDB; 191779at2157; -.
DR UniPathway; UPA00561; UER00617.
DR Proteomes; UP000258613; Chromosome.
DR Proteomes; UP000258707; Chromosome.
DR GO; GO:0031419; F:cobalamin 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:InterPro.
DR GO; GO:0019553; P:glutamate catabolic process via L-citramalate; IEA:UniProtKB-UniRule.
DR CDD; cd00245; Glm_e; 1.
DR Gene3D; 3.90.970.10; -; 1.
DR Gene3D; 3.20.20.240; Methylmalonyl-CoA mutase; 1.
DR HAMAP; MF_01923; Me_Asp_mutase_E; 1.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR006396; Glu_mut_E.
DR InterPro; IPR014714; Glu_mut_E_C_dom_sf.
DR NCBIfam; TIGR01503; MthylAspMut_E; 1.
DR Pfam; PF06368; Met_asp_mut_E; 1.
DR PIRSF; PIRSF001495; Met_asp_mut_epsi; 1.
DR SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|HAMAP-Rule:MF_01923};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|HAMAP-Rule:MF_01923};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01923};
KW Reference proteome {ECO:0000313|Proteomes:UP000258613}.
FT BINDING 62
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 64
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 96
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 119
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 145..146
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 167
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 173
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 176
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 177
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 289
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 318
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
FT BINDING 322
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01923"
SQ SEQUENCE 473 AA; 51925 MW; C7442DD6615EBE3C CRC64;
MIRDERIPSD ELRRIDEEIR SDWPTGADVD FEEAIAYHES LPERKRFADV LESADKPLLQ
PRAGVPRLDD QIELLEYLHG EGKADLLPTT IDSYTRDNEY EKAQQGLEKA RETGDDTLNG
FPAVNHGVEG CRELIEAIDA PIEVRHGTPD ARLLAAITFA GGFQSFEGGP ISYNIPYTKR
HGLEETIERW QFVDRLAGAY TQRGVRINRE PFGPLTGTLV PPSIAIAIGI VEGQLAATQG
VRSITLGYGQ VGNVVQDVAA LNALRDLANE YLPDEVVVTT VFHEWMGGFP PDEARANGVI
SLGGMTAAIA QPDKVITKSP QEFQGVPTMQ ANAAGLRTTR QVIDMAIEQN IGIDGIVEEQ
DLIERETRCL MDAIFTHGDG DVVQGTIKAF DSGALDVPFA PSDSAKGAIL PARDDDGRVR
IFEWADLEMD DDIKEIHKAR LSQRADTEGR EQSFRMVADD VDAISDGKLI GRP
//
