ID A0A1M5TYD6_9FIRM Unreviewed; 403 AA.
AC A0A1M5TYD6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Oxalate decarboxylase {ECO:0000313|EMBL:SHH55704.1};
GN ORFNames=SAMN02745823_00281 {ECO:0000313|EMBL:SHH55704.1};
OS Sporobacter termitidis DSM 10068.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Sporobacter.
OX NCBI_TaxID=1123282 {ECO:0000313|EMBL:SHH55704.1, ECO:0000313|Proteomes:UP000183995};
RN [1] {ECO:0000313|EMBL:SHH55704.1, ECO:0000313|Proteomes:UP000183995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10068 {ECO:0000313|EMBL:SHH55704.1,
RC ECO:0000313|Proteomes:UP000183995};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQXV01000001; SHH55704.1; -; Genomic_DNA.
DR RefSeq; WP_073075846.1; NZ_FQXV01000001.1.
DR AlphaFoldDB; A0A1M5TYD6; -.
DR STRING; 1123282.SAMN02745823_00281; -.
DR OrthoDB; 9801056at2; -.
DR Proteomes; UP000183995; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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.
PE 4: Predicted;
KW Manganese {ECO:0000256|PIRSR:PIRSR617774-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR617774-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000183995}.
FT DOMAIN 58..200
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT DOMAIN 236..377
FT /note="Cupin type-1"
FT /evidence="ECO:0000259|SMART:SM00835"
FT ACT_SITE 341
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-1"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 105
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 109
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 148
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 281
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 283
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 288
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT BINDING 327
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
SQ SEQUENCE 403 AA; 44604 MW; 13C3208FBF59C006 CRC64;
MYFDFQSARR NFSYIPEPIR NGWGATDPGP RDILRDLENP DMLVPPATDA GLMPNLKFSF
SDTSMVLKPG GWSREITARE MPALKTLAAV NMRLTPGGVR EVHWHEASEW SLVLTGSARV
TAVDQQGRNF IGDIHPGDLW YFPPRVSHAL QGMADGCEFI LLFDDGDFSD LNTLSLSDLF
AHYPREVLSM NFGVPASEFR TFPSGQVYIY QGTVPGPLEE EAVRSPFGPV PQTFKHELMA
QDPIATAGGS VRIADTANFH VAKTTAAALV EIKPGAMREI HWHNNNDEFQ YYLTGQGRMT
VFGENGRART FNYRAGDVGY IPVGYVHYVQ NTGNDTLWFL EAFRSEHFES ISLNQTMALT
PRSIVGSNLR AGPQFLDALR AANCPVIPCV SDNAYQADAG GMK
//
