OXBP_THEMA
ID OXBP_THEMA Reviewed; 121 AA.
AC Q9X113;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Oxalate-binding protein {ECO:0000305|PubMed:15211523};
DE AltName: Full=Putative oxalate decarboxylase {ECO:0000303|PubMed:15211523};
GN OrderedLocusNames=TM_1287 {ECO:0000312|EMBL:AAD36361.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274 {ECO:0000312|EMBL:AAD36361.1};
RN [1] {ECO:0000312|EMBL:AAD36361.1, ECO:0000312|Proteomes:UP000008183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC {ECO:0000312|Proteomes:UP000008183};
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2] {ECO:0007744|PDB:1O4T}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH MANGANESE AND
RP OXALATE, FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC {ECO:0000303|PubMed:15211523};
RX PubMed=15211523; DOI=10.1002/prot.20016;
RA Schwarzenbacher R., von Delft F., Jaroszewski L., Abdubek P., Ambing E.,
RA Biorac T., Brinen L.S., Canaves J.M., Cambell J., Chiu H.J., Dai X.,
RA Deacon A.M., DiDonato M., Elsliger M.A., Eshagi S., Floyd R., Godzik A.,
RA Grittini C., Grzechnik S.K., Hampton E., Karlak C., Klock H.E., Koesema E.,
RA Kovarik J.S., Kreusch A., Kuhn P., Lesley S.A., Levin I., McMullan D.,
RA McPhillips T.M., Miller M.D., Morse A., Moy K., Ouyang J., Page R.,
RA Quijano K., Robb A., Spraggon G., Stevens R.C., van den Bedem H.,
RA Velasquez J., Vincent J., Wang X., West B., Wolf G., Xu Q., Hodgson K.O.,
RA Wooley J., Wilson I.A.;
RT "Crystal structure of a putative oxalate decarboxylase (TM1287) from
RT Thermotoga maritima at 1.95 A resolution.";
RL Proteins 56:392-395(2004).
CC -!- FUNCTION: Binds oxalate. {ECO:0000269|PubMed:15211523}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15211523}.
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DR EMBL; AE000512; AAD36361.1; -; Genomic_DNA.
DR PIR; F72271; F72271.
DR RefSeq; NP_229091.1; NC_000853.1.
DR PDB; 1O4T; X-ray; 1.95 A; A/B=1-121.
DR PDBsum; 1O4T; -.
DR AlphaFoldDB; Q9X113; -.
DR SMR; Q9X113; -.
DR STRING; 243274.THEMA_07900; -.
DR EnsemblBacteria; AAD36361; AAD36361; TM_1287.
DR KEGG; tma:TM1287; -.
DR PATRIC; fig|243274.5.peg.1303; -.
DR eggNOG; COG0662; Bacteria.
DR InParanoid; Q9X113; -.
DR OMA; HEHVGDF; -.
DR EvolutionaryTrace; Q9X113; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0046564; F:oxalate decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0033609; P:oxalate metabolic process; ISS:UniProtKB.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR013096; Cupin_2.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF07883; Cupin_2; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..121
FT /note="Oxalate-binding protein"
FT /id="PRO_0000433802"
FT BINDING 61
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:15211523,
FT ECO:0007744|PDB:1O4T"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:15211523,
FT ECO:0007744|PDB:1O4T"
FT BINDING 68
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:15211523,
FT ECO:0007744|PDB:1O4T"
FT BINDING 70
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000269|PubMed:15211523"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:15211523,
FT ECO:0007744|PDB:1O4T"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1O4T"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1O4T"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:1O4T"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1O4T"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:1O4T"
FT TURN 37..42
FT /evidence="ECO:0007829|PDB:1O4T"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:1O4T"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:1O4T"
FT STRAND 65..81
FT /evidence="ECO:0007829|PDB:1O4T"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:1O4T"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:1O4T"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1O4T"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1O4T"
FT STRAND 112..120
FT /evidence="ECO:0007829|PDB:1O4T"
SQ SEQUENCE 121 AA; 13270 MW; A13DA3516146A62E CRC64;
MKEGTGMVVR SSEITPERIS NMRGGKGEVE MAHLLSKEAM HNKARLFARM KLPPGSSVGL
HKHEGEFEIY YILLGEGVFH DNGKDVPIKA GDVCFTDSGE SHSIENTGNT DLEFLAVIIL
L
