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Database: UniProt
Entry: E8X6Q2_GRATM
LinkDB: E8X6Q2_GRATM
Original site: E8X6Q2_GRATM 
ID   E8X6Q2_GRATM            Unreviewed;       416 AA.
AC   E8X6Q2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Bicupin, oxalate decarboxylase family {ECO:0000313|EMBL:ADW71202.1};
DE            EC=4.1.1.2 {ECO:0000313|EMBL:ADW71202.1};
GN   OrderedLocusNames=AciX9_3926 {ECO:0000313|EMBL:ADW71202.1};
OS   Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9).
OG   Plasmid pACIX902 {ECO:0000313|EMBL:ADW71202.1,
OG   ECO:0000313|Proteomes:UP000000343}.
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=1198114 {ECO:0000313|Proteomes:UP000000343};
RN   [1] {ECO:0000313|Proteomes:UP000000343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP5ACTX9 {ECO:0000313|Proteomes:UP000000343};
RC   PLASMID=Plasmid pACIX902 {ECO:0000313|Proteomes:UP000000343};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Ovchinnikova G., Pagani I., Rawat S.R., Mannisto M.,
RA   Haggblom M.M., Woyke T.;
RT   "Complete sequence of plasmid2 of Acidobacterium sp. MP5ACTX9.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR617774-2};
CC       Note=Binds 2 manganese ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR617774-2};
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DR   EMBL; CP002482; ADW71202.1; -; Genomic_DNA.
DR   RefSeq; WP_013582220.1; NC_015065.1.
DR   AlphaFoldDB; E8X6Q2; -.
DR   SMR; E8X6Q2; -.
DR   KEGG; acm:AciX9_3926; -.
DR   HOGENOM; CLU_030515_2_0_0; -.
DR   OrthoDB; 1973590at2; -.
DR   Proteomes; UP000000343; Plasmid pACIX902.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046564; F:oxalate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0033609; P:oxalate metabolic process; IEA:InterPro.
DR   CDD; cd20305; cupin_OxDC_C; 1.
DR   CDD; cd20304; cupin_OxDC_N; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR017774; Bicupin_oxalate_deCO2ase/Oxase.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   NCBIfam; TIGR03404; bicupin_oxalic; 1.
DR   PANTHER; PTHR35848:SF6; CUPIN 2 CONSERVED BARREL DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR35848; OXALATE-BINDING PROTEIN; 1.
DR   Pfam; PF00190; Cupin_1; 2.
DR   SMART; SM00835; Cupin_1; 2.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:ADW71202.1};
KW   Manganese {ECO:0000256|PIRSR:PIRSR617774-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR617774-2}; Plasmid {ECO:0000313|EMBL:ADW71202.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000343}.
FT   DOMAIN          84..225
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   DOMAIN          261..404
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   REGION          44..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        368
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-1"
FT   BINDING         127
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         129
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         133
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         172
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         308
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         310
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         315
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         354
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
SQ   SEQUENCE   416 AA;  45994 MW;  BD2DDA4FA2071B12 CRC64;
     MSDNQNNPLS RRKFLGNTSA ALAAFGALQV ASGQEAVPIR SKDHHLINET ETQPKNKMLD
     DQNPSSNWPP TTDAGGQQPF KYSFSLSHKR IEGGGWTRQV TVRDLPISKK MAGVQMRLIK
     GGIRELHWHV GAEWAFMIGG SARITAVDQQ GRAFVDDVNE GDLWVFPGGI PHSIQGLGPD
     GCVFLLVFDD GNFNEFETFL LTDWLHHTPP EVLAKNFDVP ASTFANVPPK ELFIFERDLP
     RPLAEEKHQV EAVTGPVPNT FAFFTSKMAP TKVTKGGSVK IIDAKNFPAS NIAAAIVTLK
     PGGLRELHWH PNEDEWQYYV KGSGRMSVFA AGGRARTMDF QAGDVGYIDK STPHFVENTG
     DEDLVFLEVF PTPHYEDISL AEWLAHTPSR LVNEHLGVGE DFLNKISKKE AVVDPE
//
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