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Database: UniProt
Entry: A0A0Q5E5N0_9MICO
LinkDB: A0A0Q5E5N0_9MICO
Original site: A0A0Q5E5N0_9MICO 
ID   A0A0Q5E5N0_9MICO        Unreviewed;       405 AA.
AC   A0A0Q5E5N0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Cupin {ECO:0000313|EMBL:KQQ52934.1};
GN   ORFNames=ASF68_11850 {ECO:0000313|EMBL:KQQ52934.1};
OS   Plantibacter sp. Leaf314.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Plantibacter.
OX   NCBI_TaxID=1736333 {ECO:0000313|EMBL:KQQ52934.1, ECO:0000313|Proteomes:UP000051200};
RN   [1] {ECO:0000313|EMBL:KQQ52934.1, ECO:0000313|Proteomes:UP000051200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ52934.1,
RC   ECO:0000313|Proteomes:UP000051200};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ52934.1, ECO:0000313|Proteomes:UP000051200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ52934.1,
RC   ECO:0000313|Proteomes:UP000051200};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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   -!- 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:KQQ52934.1}.
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DR   EMBL; LMOB01000001; KQQ52934.1; -; Genomic_DNA.
DR   RefSeq; WP_056010454.1; NZ_LMOB01000001.1.
DR   AlphaFoldDB; A0A0Q5E5N0; -.
DR   STRING; 1736333.ASF68_11850; -.
DR   OrthoDB; 1973590at2; -.
DR   Proteomes; UP000051200; 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:UP000051200}.
FT   DOMAIN          71..212
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   DOMAIN          249..391
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        355
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-1"
FT   BINDING         114
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         116
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         120
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         159
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         295
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         297
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         302
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
FT   BINDING         341
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617774-2"
SQ   SEQUENCE   405 AA;  44603 MW;  A9ED8877F4B7F9BC CRC64;
     MDSTDATVPH HDAPRLGNPD LPAEGEENTL LHPQSTRMTG PQNPAIASQF PNQIDAPGTD
     ISTQAFFWSS FNISPRRVQD GGWAREVTKQ DFAISDEIAG VNMYLEAGGI RELHWHQTAE
     WAVMTRGKCR VTTLSRSGLP SVEDVEEGDL WFFPAGTPHS LQGLGPDGAE FVLAFDDGEQ
     SESNTLLLTD WFAHTPPDVL AKNFGVAQET FSDIPLHNLW IFPGDEPGPL AKDQEDAGVE
     WGASEPIIFR LSRSKPLHRN SGGSIQIADS TNFPLSQSVA AALVTVEPGS MRELHWHPNA
     DEWQYYLRGS ARMTVFNTGP HANTTDFRPG DIGVVKRNLG HYVENTGDDV LQFLEVFRTD
     RYEEVSLANW LAHVPPSLVA AHLNIDEATL ATFPREAQGI TPLRP
//
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