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Database: UniProt
Entry: A0A0J1CX59_9BURK
LinkDB: A0A0J1CX59_9BURK
Original site: A0A0J1CX59_9BURK 
ID   A0A0J1CX59_9BURK        Unreviewed;      1153 AA.
AC   A0A0J1CX59;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   03-MAY-2023, entry version 23.
DE   SubName: Full=IMP dehydrogenase {ECO:0000313|EMBL:KLU25155.1};
GN   ORFNames=EOS_16325 {ECO:0000313|EMBL:KLU25155.1};
OS   Caballeronia mineralivorans PML1(12).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU25155.1, ECO:0000313|Proteomes:UP000035963};
RN   [1] {ECO:0000313|EMBL:KLU25155.1, ECO:0000313|Proteomes:UP000035963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX   PubMed=26205858;
RA   Uroz S., Oger P.;
RT   "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT   Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT   Ability.";
RL   Genome Announc. 3:e00798-15(2015).
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:KLU25155.1}.
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DR   EMBL; AEJF01000104; KLU25155.1; -; Genomic_DNA.
DR   RefSeq; WP_047847706.1; NZ_AEJF01000104.1.
DR   AlphaFoldDB; A0A0J1CX59; -.
DR   PATRIC; fig|908627.4.peg.3650; -.
DR   OrthoDB; 9804872at2; -.
DR   Proteomes; UP000035963; Unassembled WGS sequence.
DR   Gene3D; 3.10.620.30; -; 1.
DR   InterPro; IPR013589; Bac_transglu_N.
DR   InterPro; IPR018667; DUF2126.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   PANTHER; PTHR33490; BLR5614 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR33490:SF1; SLL1233 PROTEIN; 1.
DR   Pfam; PF08379; Bact_transglu_N; 1.
DR   Pfam; PF09899; DUF2126; 1.
DR   Pfam; PF01841; Transglut_core; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   4: Predicted;
FT   DOMAIN          172..248
FT                   /note="Transglutaminase-like"
FT                   /evidence="ECO:0000259|SMART:SM00460"
FT   REGION          582..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1153 AA;  129475 MW;  D5289B3B5A5F4927 CRC64;
     MSIRVALNHV THYRYDRLVG LSPQVVRLRP APHCRTPIVS YSMRVEPAEH FINWQQDAFA
     NYQARLVFPE KTREFKITVD LVAEMAVYNP FDFFLEPYAE KFPFEYEPEL AAELAPYLIK
     REPTPLLAKF VDSIDKTAKV TADFLVELNQ RLQHDIGYVI RMEPGVQTPE ETLEKALGSC
     RDTGWLLVET LRQLGLAARF VSGYLIQLTP DQKSLDGPSG TEVDFTDLHA WCEVFLPGAG
     WIGLDPTSGL LAGEGHIPVA CTPEPGSAAP IFGAVDESEV EFEHIMQIQR VLETPRVTKP
     YTEEVWSAVQ TMGAQVDQQL NDMDVRLTMG GEPTFVAVTD RDAAEWNTDA LGPTKRGYAV
     SLMDKLRARY GVGGFLHLGQ GKWYPGEQLP RWAMSLFWRA DGEPIWVDPT LFADERDPGH
     YTAEDARRFI EHLADKVSLD ASYIQPGYED TFYYLWRERR LPVNVDPFES ELDDEMERMR
     LRRVFDAGLS QVTGYVLPIA RERDIPMQAP AWVSGPWFFR DGRMYLIPGD SPMGYRLPLE
     SLPWVSAGDY PYQHPHDPFG PPVPLREAME LRMQYRGGVV PGSGIEGRAE GEGATGAGAG
     SGAVASTGQR PAASTREPSR GESASWIRRT ALCVEARDPA RAAGPDVEEK SFGSGKSLLH
     VFMPPLTELD DYLDLLAAIE ATAADLHMKV VIEGYPPPRD ARLKMLQVTP DPGVIEVNIH
     PASSWDQLVD HTEYLYQSAH ESYLSTEKFM TDGRHTGTGG GNHFVLGGAT PADSPFLRRP
     DLLASLIAYF INHPSMSYLF SGLFLGPTSQ APRVDEARND QLYELEIAFK EIEHQLERLG
     GRDSAQLPPW LIDRTLRNLL IDVTGNTHRA EFCIDKLYSP DGPTGRLGLL ELRGFEMPPH
     ARMSLVQQLL LRALVARFWD KPYTTRLTRW GTELHDRFLL GTFIEMDFHD VIADLNEAGY
     AFDAAWFAPH FEFRFPLVGA VQTNGIELVV RSALEPWHVM GEQGAPGGTV RYVDSSVERL
     EVRVLGLNDN RHVVTVNGVP LPLQPTGRVS EHVAGVRFRA WSQPTALHPS IGVDAPLTFD
     IVDTWSNRSI GGCRYHVAHP GGRNYVTYPV NAYEAESRRR SRFFRIGHTP GRMVVEEPKR
     SLEFPFTLDL RRR
//
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