GLME_HALMA
ID GLME_HALMA Reviewed; 487 AA.
AC Q5V466;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Glutamate mutase epsilon subunit {ECO:0000255|HAMAP-Rule:MF_01923};
DE EC=5.4.99.1 {ECO:0000255|HAMAP-Rule:MF_01923};
DE AltName: Full=Glutamate mutase E chain {ECO:0000255|HAMAP-Rule:MF_01923};
DE AltName: Full=Glutamate mutase large subunit {ECO:0000255|HAMAP-Rule:MF_01923};
DE AltName: Full=Methylaspartate mutase {ECO:0000255|HAMAP-Rule:MF_01923};
GN Name=glmE {ECO:0000255|HAMAP-Rule:MF_01923}; Synonyms=mamB;
GN OrderedLocusNames=rrnAC0685;
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_01923};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
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_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:0000255|HAMAP-Rule:MF_01923}.
CC -!- SIMILARITY: Belongs to the methylaspartate mutase GlmE subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01923}.
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DR EMBL; AY596297; AAV45686.1; -; Genomic_DNA.
DR RefSeq; WP_007190471.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V466; -.
DR SMR; Q5V466; -.
DR STRING; 272569.rrnAC0685; -.
DR EnsemblBacteria; AAV45686; AAV45686; rrnAC0685.
DR GeneID; 40151725; -.
DR KEGG; hma:rrnAC0685; -.
DR PATRIC; fig|272569.17.peg.1435; -.
DR eggNOG; arCOG06231; Archaea.
DR HOGENOM; CLU_029922_0_0_2; -.
DR OMA; VIVKTPH; -.
DR BioCyc; MetaCyc:MON-16254; -.
DR UniPathway; UPA00561; UER00617.
DR Proteomes; UP000001169; Chromosome I.
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:UniProtKB-UniRule.
DR GO; GO:0019553; P:glutamate catabolic process via L-citramalate; IEA:UniProtKB-UniPathway.
DR CDD; cd00245; Glm_e; 1.
DR Gene3D; 3.90.970.10; -; 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 Pfam; PF06368; Met_asp_mut_E; 1.
DR PIRSF; PIRSF001495; Met_asp_mut_epsi; 1.
DR SUPFAM; SSF51703; SSF51703; 1.
DR TIGRFAMs; TIGR01503; MthylAspMut_E; 1.
PE 3: Inferred from homology;
KW Cobalamin; Cobalt; Isomerase; Reference proteome.
FT CHAIN 1..487
FT /note="Glutamate mutase epsilon subunit"
FT /id="PRO_0000429441"
FT REGION 465..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 64
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 96
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 119
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 145..146
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 167
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 173
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 176
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 177
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 289
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 318
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
FT BINDING 322
FT /ligand="adenosylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:18408"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01923"
SQ SEQUENCE 487 AA; 52648 MW; 5E7A78E384E4D539 CRC64;
MPTDERLSDD QLQRIANDLR DNWHTGREVD FEEAIAFHES LPASKQFAQV LESADQPLLQ
PRAGVPCLEE QIDLLRYLQD EGGADLLPTT IDSYTRDNEY EKAEEGLAAS RGSDENELNG
FPAVNHGVED CRRLIRALDA PVEVRHGTPD ARLLAMVTLA GGFQSFEGGP ISYNIPYTKR
HDLATTIEHW QFVDRLCGAY TERGVTINRE PFGPLTGTLV PPSIAIAVML VEGELAATQG
VRSLTLGYGQ VGNLVQDVAA LRALRKLGNE YLRDEVTVTT VFHEWMGGFP PDEARANGVI
SLGGATAAVA QPDKVITKSA QEFQGVPTKE ANAAGLRTTR QLIDMMIEQD IDLGGIDEEQ
ALIERETRAL MDAIYEAGDG DVAQGVINAF DSGALDVPFA PSDAAKGAVL PARDDDGRVR
IFEFADLALP DDIKEIHAAR LGERAETEGR DQSFRMVADD VDAISDGKLI GRPGGDNSPA
GGASDAD
