ID K7RU85_ACIA4 Unreviewed; 579 AA.
AC K7RU85;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Thiamine pyrophosphate enzyme {ECO:0000313|EMBL:AFV89951.1};
GN OrderedLocusNames=PACID_21650 {ECO:0000313|EMBL:AFV89951.1};
OS Acidipropionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 / JCM
OS 6432 / NBRC 12425 / NCIMB 8070 / 4) (Propionibacterium acidipropionici).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Acidipropionibacterium.
OX NCBI_TaxID=1171373 {ECO:0000313|EMBL:AFV89951.1, ECO:0000313|Proteomes:UP000000214};
RN [1] {ECO:0000313|EMBL:AFV89951.1, ECO:0000313|Proteomes:UP000000214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070
RC {ECO:0000313|Proteomes:UP000000214};
RX PubMed=23083487; DOI=10.1186/1471-2164-13-562;
RA Parizzi L.P., Grassi M.C., Llerena L.A., Carazzolle M.F., Queiroz V.L.,
RA Lunardi I., Zeidler A.F., Teixeira P.J., Mieczkowski P., Rincones J.,
RA Pereira G.A.;
RT "The genome sequence of Propionibacterium acidipropionici provides insights
RT into its biotechnological and industrial potential.";
RL BMC Genomics 13:562-562(2012).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP003493; AFV89951.1; -; Genomic_DNA.
DR RefSeq; WP_015070851.1; NC_019395.1.
DR AlphaFoldDB; K7RU85; -.
DR STRING; 1171373.PACID_21650; -.
DR KEGG; pbo:PACID_21650; -.
DR PATRIC; fig|1171373.8.peg.2140; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_11; -.
DR Proteomes; UP000000214; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR047211; POXB-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..528
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 579 AA; 61817 MW; A2210DF8C3E53F32 CRC64;
MNVAEQLVQQ LVDAGVRRIY GIVGDSLNPI VEAVRKTGGS AKGGIDWVHV RHEEAAAFSA
AAEAQLTGEL AVCAGSCGPG NMHLINGLYD AHRSGAPVLA IASHIPSVQI GSDFFQETHP
DRLFTECASY CELISTAQQA PRVINSAIRH ASALDDVAVI TISSDVSGAK AVAPTPVYVP
ARRAVIAPNP EDLTQLVKLL NDSKKVAIFA GLGVEGAHDE VIALADKLKA PIGHSLRGKD
FIQYDNPFDV GMTGLLGYGA AAEGMKDADV LLLLGTDFPY NQFLPDTLTV QVDSHPEKLG
RRTDVSFPVQ ADVKPLVEAL LPLVKEHDDK FLKATVKRHA RIMNAPVGSY TRNVEHMKPI
HPEYVAHVLN EVADKDAIFT ADTGMCNVWT ARYIDPLGTR RLIGSFKHGS MANALPMAIG
AQVSHPGRQV ISVSGDGGLS MLLGELVTAR MHNLPLKVVV FNNSTLGMVK LEQYVGGLPD
FGTDVHDVNY AGVAKAMGFH ARRVDDAKDI REALTEALQA DGPALVEVLT DPNALSLPPE
IKGEMLIGFA TAMSKVVFNR GAGEVVSMAT SNMRNIPRP
//
