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Database: UniProt
Entry: A0A3S0BMF7_9BACL
LinkDB: A0A3S0BMF7_9BACL
Original site: A0A3S0BMF7_9BACL 
ID   A0A3S0BMF7_9BACL        Unreviewed;       387 AA.
AC   A0A3S0BMF7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Muconate cycloisomerase {ECO:0000313|EMBL:RTE09870.1};
GN   ORFNames=EJQ19_10065 {ECO:0000313|EMBL:RTE09870.1};
OS   Paenibacillus whitsoniae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2496558 {ECO:0000313|EMBL:RTE09870.1, ECO:0000313|Proteomes:UP000276128};
RN   [1] {ECO:0000313|EMBL:RTE09870.1, ECO:0000313|Proteomes:UP000276128}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MER 54 {ECO:0000313|EMBL:RTE09870.1,
RC   ECO:0000313|Proteomes:UP000276128};
RA   Seuylemezian A., Vaishampayan P.;
RT   "Bacillus ochoae sp. nov., Paenibacillus whitsoniae sp. nov., Paenibacillus
RT   spiritus sp. nov. Isolated from the Mars Exploration Rover during
RT   spacecraft assembly.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR633977-3};
CC       Note=Binds 2 magnesium ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR633977-3};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RTE09870.1}.
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DR   EMBL; RXHU01000025; RTE09870.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S0BMF7; -.
DR   OrthoDB; 9775391at2; -.
DR   Proteomes; UP000276128; Unassembled WGS sequence.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   InterPro; IPR034593; DgoD-like.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR033977; Galactarate_dehydratase_2.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   PANTHER; PTHR48080; D-GALACTONATE DEHYDRATASE-RELATED; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDG00309; galactarate_dehydratase; 1.
DR   SFLD; SFLDF00162; galactarate_dehydratase_2; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:RTE09870.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR633977-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR633977-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276128}.
FT   DOMAIN          20..121
FT                   /note="Mandelate racemase/muconate lactonizing enzyme N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02746"
FT   DOMAIN          149..360
FT                   /note="Enolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13378"
FT   ACT_SITE        90
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633977-1"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633977-1"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633977-2"
FT   BINDING         42
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633977-3"
FT   BINDING         45
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633977-3"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633977-2"
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633977-3"
FT   BINDING         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633977-3"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633977-3"
FT   BINDING         294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633977-2"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633977-3"
FT   BINDING         383
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633977-2"
FT   SITE            162
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR633977-4"
SQ   SEQUENCE   387 AA;  43271 MW;  F98C0AC0C155F54A CRC64;
     MKITNILLDV VSIPRHTGFV CQHAIVRVMT DEGIVGIGEM SDFSHLPKYS VDVRDLQATL
     QASLVGRDPF ELIAINREMA EMFPETMYYY EKGTFIRCGI DIALHDLVGK ALGVNISTLL
     GGRVRDKLKV CYPIFRSRTL EEVDANVDVV RKRLAQGFDV FRLYAGVNPD ADEAFLDRVR
     QEFGSRVTIK SLDYSHLLDW KSALRTTKRL EPYGVQLVES PAYRNDFEGL RNFRMGVDLP
     VSEHVWSFKQ LQDMIRYDSV DIFNIALIFI GGFQAARKAA AAAEISGKGV LIGTTQELSF
     GTAAQAIFGA SLTNLNAISD PTGPELYVDD VTTEPVRYEN GYLLVPEADK PGLGMDIDWE
     KVERLRVEGF SWGAQKVANL QDRTRGS
//
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