ID A1VPE3_POLNA Unreviewed; 580 AA.
AC A1VPE3;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Transcriptional regulator, Fis family {ECO:0000313|EMBL:ABM37521.1};
GN OrderedLocusNames=Pnap_2213 {ECO:0000313|EMBL:ABM37521.1};
OS Polaromonas naphthalenivorans (strain CJ2).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM37521.1, ECO:0000313|Proteomes:UP000000644};
RN [1] {ECO:0000313|Proteomes:UP000000644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644};
RX PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT tar-contaminated sediment, reveals physiological and metabolic versatility
RT and evolution through extensive horizontal gene transfer.";
RL Environ. Microbiol. 11:2253-2270(2009).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP000529; ABM37521.1; -; Genomic_DNA.
DR AlphaFoldDB; A1VPE3; -.
DR STRING; 365044.Pnap_2213; -.
DR KEGG; pna:Pnap_2213; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_4_4; -.
DR Proteomes; UP000000644; 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; cd00568; TPP_enzymes; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 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; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000644};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 23..136
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 213..348
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 406..555
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 580 AA; 62250 MW; 04C4B58309F7C7EB CRC64;
MAAIVRDGRG QGTIKRMTQQ LAGHLLVDCL LAQGVTHAFG VPGESYLAVL DGLHARRDQI
RFITCRQEGG AAFMAEAHGK LTGRPGVCMV TRGPGATNAS IGVHTAFQDS TPMVLLVGDV
ASDCRDREAF QEVDYSSFFG PSTKGFAKRV ERIDDADRIP EYVARAFATA MNGRPGPVVL
VLPEDMLTRM TAARPLPRVE AVQAWSDPGA LRTLREMLLA SKQPLIIAGG GGWTPQSAQA
LQRFAENWKL PVGNAFRFQD TFDNHHPLYA GDVGIGLSPK LAARVKASDL IIAIGPRLGE
MTTGNYTLIE APRPKQKLVH IHASAEELNR VFQADLAINA TMNAAARSLE VLSAPVSVPW
EAWTASANED YLANLVPQAL PGDVDMPAIV GLLQRYLPAD AVLTNGAGNF ASWIHRFFKH
HGLAKGHKTQ LAPTVGAMGY GVPAGIAAAI TTGRVAFTIA GDGDFLMNGQ ELATAVQHGA
KSIIVLLNNG MYGTIRMHQE KQYPQHESGS RLNNPDFAAL ARAYGYAGVR ITRTDEFEAE
LLAALDRSEG TLIEVTLDPE VITTRATLSS ITQGALKQKL
//
