ID   F5YMZ0_TREPZ            Unreviewed;       685 AA.
AC   F5YMZ0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Oxaloacetate decarboxylase alpha subunit {ECO:0000313|EMBL:AEF84478.1};
DE            EC=4.1.1.3 {ECO:0000313|EMBL:AEF84478.1};
GN   Name=oadA {ECO:0000313|EMBL:AEF84478.1};
GN   OrderedLocusNames=TREPR_1676 {ECO:0000313|EMBL:AEF84478.1};
OS   Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF84478.1, ECO:0000313|Proteomes:UP000009223};
RN   [1] {ECO:0000313|Proteomes:UP000009223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC   {ECO:0000313|Proteomes:UP000009223};
RA   Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA   Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA   Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA   Paulsen I.T.;
RT   "Complete sequence of Treponema primitia strain ZAS-2.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEF84478.1, ECO:0000313|Proteomes:UP000009223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC   {ECO:0000313|Proteomes:UP000009223};
RX   PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA   Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT   "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT   spirochete species in co-culture.";
RL   ISME J. 5:1133-1142(2011).
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DR   EMBL; CP001843; AEF84478.1; -; Genomic_DNA.
DR   RefSeq; WP_015708447.1; NC_015578.1.
DR   AlphaFoldDB; F5YMZ0; -.
DR   STRING; 545694.TREPR_1676; -.
DR   KEGG; tpi:TREPR_1676; -.
DR   eggNOG; COG0511; Bacteria.
DR   eggNOG; COG5016; Bacteria.
DR   HOGENOM; CLU_000395_4_3_12; -.
DR   OrthoDB; 9807469at2; -.
DR   Proteomes; UP000009223; Chromosome.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 2.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 2.40.50.100; -; 2.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005776; OadA.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR01108; oadA; 1.
DR   PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:AEF84478.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009223}.
FT   DOMAIN          4..264
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          609..685
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          582..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   685 AA;  72065 MW;  E0F9F2A5E447DFF2 CRC64;
     MAKVQLTDLV LRDAHQSLIA TRMVTADMLP IAEKLDKVGY YALEAWGGAT FDTCIRFLNE
     DPWERLKKLK AALPNTKIMM LLRGQNLLGY RHYADDVVAK FVEIAAKDGV DIFRIFDAVN
     DPRNFQAATA AAKKTGKHIQ AAISYAVTPF HTIEKYAELA KQYADIGADS ICIKDMSGLL
     KPYEAYSLVK AIKKVTDLPI EIHSHATTGM SVATLTKAAE AGAEILDTVI SSLAMGTSHS
     PTETMVEIFR GTEFDTGLDI KLLLEIAAYF RDVRKNYKKF ESSFQGADTR ILLSQVPGGM
     LSNLEGQLKE QGAADKIDDV LKEIAVVQKD SGYPPLVTPT SQIVGTQAVF NVLFGRYNKL
     SGEFQDLLAG KYGACPAPKN QDVVKKALEA LKLEKEVTHR PADDIPPEYS KLEDEAKKVL
     GTSSVSVEDV LTYAMFPKVA PEFFKKRSQG PVVFKPEPAA PAGGAAPAAA PGQAAKYVVN
     VNGANYNVVV QPAGTVAIAP APGAAASSGA APGAARSGGG VTIPAPVAGT VLRYAVNEGE
     EVKSGTTVLI IESMKMELEI KATSAGPIHF LVPTGTQVAS QQPVAEVGGS GGSEPVPAAA
     PEAAPAAPEA AAPSSGGTVI PSPVAGTVLR YAVNEGAAVK PGDTVVIIES MKMELEIKAT
     AAGAVHFLAP TGAQVASQQP LAEIG
//