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Database: UniProt
Entry: Q30UF1_SULDN
LinkDB: Q30UF1_SULDN
Original site: Q30UF1_SULDN 
ID   Q30UF1_SULDN            Unreviewed;       318 AA.
AC   Q30UF1;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Pyruvate:acceptor oxidoreductase beta subunit {ECO:0000313|EMBL:ABB43380.1};
GN   OrderedLocusNames=Suden_0099 {ECO:0000313|EMBL:ABB43380.1};
OS   Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS   denitrificans (strain ATCC 33889 / DSM 1251)).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=326298 {ECO:0000313|EMBL:ABB43380.1, ECO:0000313|Proteomes:UP000002714};
RN   [1] {ECO:0000313|EMBL:ABB43380.1, ECO:0000313|Proteomes:UP000002714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33889 / DSM 1251 {ECO:0000313|Proteomes:UP000002714};
RX   PubMed=18065616; DOI=10.1128/AEM.01844-07;
RA   Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA   Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA   Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA   Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA   Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA   Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT   "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT   denitrificans.";
RL   Appl. Environ. Microbiol. 74:1145-1156(2008).
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DR   EMBL; CP000153; ABB43380.1; -; Genomic_DNA.
DR   RefSeq; WP_011371735.1; NC_007575.1.
DR   AlphaFoldDB; Q30UF1; -.
DR   STRING; 326298.Suden_0099; -.
DR   KEGG; tdn:Suden_0099; -.
DR   eggNOG; COG1013; Bacteria.
DR   HOGENOM; CLU_058423_0_0_7; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000002714; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd03376; TPP_PFOR_porB_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR42897; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR   PANTHER; PTHR42897:SF2; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:ABB43380.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002714}.
FT   DOMAIN          53..222
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          151..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   318 AA;  35631 MW;  996113263C49CCF5 CRC64;
     MSEMKNIKNL KEFSTSADRF EGANLLCPGC AHSIIVREVL NATNDDLVLS ASTGCLEVCT
     AVYPYTSWDA SWIHIGFENS STAVAGAETM YKALKKKGRL KQPERNPKFV SFAGDGASYD
     IGFQWISGCM ERGHNMMHVV LDNEVYANTG GQRSSSTPIG SSATTSPAGR VSYGEKRNKK
     DMMSIMAAHG IPYAAQVAPN KWKDMVKKIQ HGLSVEGPVF INAVSPCTTE WKFDPKDTMH
     ITDLATDSLV FPLYEIIDGT ELNITYRPKN VVPVEEYLAA QGRFKHLFKD EYKYLIKEWQ
     ERVDAKWAYL QRREESRV
//
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