ID Q3JDV2_NITOC Unreviewed; 601 AA.
AC Q3JDV2;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:ABA56994.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:ABA56994.1};
GN OrderedLocusNames=Noc_0471 {ECO:0000313|EMBL:ABA56994.1};
OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS 11848 / C-107).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=323261 {ECO:0000313|EMBL:ABA56994.1, ECO:0000313|Proteomes:UP000006838};
RN [1] {ECO:0000313|Proteomes:UP000006838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19707 / BCRC 17464 / NCIMB 11848 / C-107
RC {ECO:0000313|Proteomes:UP000006838};
RX PubMed=16957257; DOI=10.1128/AEM.00463-06;
RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA Vergez L.M., Ward B.B.;
RT "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL Appl. Environ. Microbiol. 72:6299-6315(2006).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP000127; ABA56994.1; -; Genomic_DNA.
DR RefSeq; WP_002812710.1; NC_007484.1.
DR AlphaFoldDB; Q3JDV2; -.
DR STRING; 323261.Noc_0471; -.
DR KEGG; noc:Noc_0471; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_6; -.
DR InParanoid; Q3JDV2; -.
DR Proteomes; UP000006838; Chromosome.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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 Pyruvate {ECO:0000313|EMBL:ABA56994.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006838};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:ABA56994.1}.
FT DOMAIN 5..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 601 AA; 66105 MW; AFBA36A3989F71CB CRC64;
MSQIVSDFLL HRLNEWGINR IYGYPGDGIN GIVGALDRLQ DRIEFIQTRH EEMAAFMACA
HAKFTGEVGV CLATSGPGAI HLLNGLYDAK LDHQPVVAIV GQQSRAALGG DYQQEVDLIS
LFKDVAHEYV HMCATPAQVR HLIDRAVRIA KTERTVTCLI FPNDVQELEA VEKPPRAHGT
IHSSTGYTIP RVIPHQQDLQ QAAEVLNRGK KVAILVGAGA LGATDEVIQV AELLGAGVAK
ALLGKGALPD ELPFVTGAIG LLGTKPSWEL MDGCDTLLMI GSSFPYSEFL PEEGQARGVQ
IDLDGRMLGI RYPMEVNLVG DSAETLRALI PLLTRKTNRA WREKIEKDVA QWWQVLESRA
MHDADPINPQ RVFWELSSRL PDNCIISSDS GSAANWYARD LKIRRGMMCS LSGGLATMGP
GVPYAIAAKF AFPDRVAIAL VGDGAMQMNG NSELVTAAKY WQQWQDPRLI VLVLNNRDLN
QVTWEQRVMS GDPKFEGSQS LPDFPYARYA ELLGFKGIRV DRPESIGPAW EEALAADRPV
ILEAYTDGNV PPLPPHIKLE QAKAYVSALL HRDPEAINII KQSIKEIKES WFSSGQEEKG
N
//