ID D5RRV6_9PROT Unreviewed; 189 AA.
AC D5RRV6;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Thiamine pyrophosphate enzyme, N-terminal TPP binding domain protein {ECO:0000313|EMBL:EFH09946.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:EFH09946.1};
DE Flags: Fragment;
GN ORFNames=HMPREF0731_3818 {ECO:0000313|EMBL:EFH09946.1};
OS Pseudoroseomonas cervicalis ATCC 49957.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Pseudoroseomonas.
OX NCBI_TaxID=525371 {ECO:0000313|EMBL:EFH09946.1, ECO:0000313|Proteomes:UP000005324};
RN [1] {ECO:0000313|EMBL:EFH09946.1, ECO:0000313|Proteomes:UP000005324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49957 {ECO:0000313|EMBL:EFH09946.1,
RC ECO:0000313|Proteomes:UP000005324};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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:EFH09946.1}.
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DR EMBL; ADVL01000720; EFH09946.1; -; Genomic_DNA.
DR AlphaFoldDB; D5RRV6; -.
DR HOGENOM; CLU_1437357_0_0_5; -.
DR Proteomes; UP000005324; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR PANTHER; PTHR18968:SF169; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005324};
KW Transferase {ECO:0000313|EMBL:EFH09946.1}.
FT DOMAIN 4..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT REGION 169..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 189
FT /evidence="ECO:0000313|EMBL:EFH09946.1"
SQ SEQUENCE 189 AA; 20044 MW; 5AC4A9CD248A67C2 CRC64;
MRQNGAEWLA RSIARSGQSH VFFIDAVLRP TLMALQAEGV QPVLAHSEKG AAYMADGYAR
IAGRPGIVAA QSVGAANLAA ALQDAWLARA PLLALTGRKT PAAQHRNAYQ EVAHAPLFAP
VTKFSAAVES TAELPRLFRQ AWAAAVSASP RPAHLDLNGL MGEVVEQGEA PEPPAELGAW
RAPRHRPLP
//