ID Q2G5Q8_NOVAD Unreviewed; 563 AA.
AC Q2G5Q8;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Thiamine pyrophosphate enzyme-like TPP-binding protein {ECO:0000313|EMBL:ABD26815.1};
GN OrderedLocusNames=Saro_2379 {ECO:0000313|EMBL:ABD26815.1};
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238 {ECO:0000313|EMBL:ABD26815.1, ECO:0000313|Proteomes:UP000009134};
RN [1] {ECO:0000313|Proteomes:UP000009134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC / F199 {ECO:0000313|Proteomes:UP000009134};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP000248; ABD26815.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2G5Q8; -.
DR STRING; 279238.Saro_2379; -.
DR KEGG; nar:Saro_2379; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_2_5; -.
DR Proteomes; UP000009134; 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; cd02010; TPP_ALS; 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:SF129; ACETOLACTATE SYNTHASE; 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:UP000009134};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 18..134
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 203..335
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 395..541
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 563 AA; 61956 MW; 7878C616F87F7C5F CRC64;
MAARLPQWER REMADGKKAS DLFIECLEEE GCEYIFGVPG EENLDFLDSL SRSKKIRLVL
TRHEQGAGFM AATYGRHTGK TGVCIATLGP GATNFVTAAA YATLGGMPML MITGQKPIKK
SKQGRFQILD VVSMMGPITK FTHQMASSDN IPSRVREAYR LAEEEKPGAT HIELPEDIAD
EHTTSVPLKR SLVRRPNADA KSVAQAVHAL QNAKAPVLVI GAGANRKMTG KMLLEFVEKT
GIPFLTTQLG KGVIDERHPK FLGCAALSSG DFVHRAVEDA DIIINVGHDV IEKPPFFMRE
GGTPVIHVST KTAEVDPVYF PSIEVIGDIA NAIWQMKEAI TPNPAWNFDH MLAYRAAEVA
HTAPLAADMR FPVFPPHLVQ QVRDCMPEDG IICLDNGVYK IWFARGYTAY KPNTVLLDNA
LATMGAGLPS AMMSAMLYPD RKVMAICGDG GFMMNSQEME TAVRLGLNLT VLILNDSAYG
MIRWKQANMG FEDFGLTYNN PDFVKYADSY GAKGYRVESA EHLEKLLAHC RDTPGVHLID
CPVDYSENDQ ILNKDIKELS KAL
//
