ID Q2IPR2_ANADE Unreviewed; 586 AA.
AC Q2IPR2;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE SubName: Full=Thiamine pyrophosphate enzyme {ECO:0000313|EMBL:ABC80790.1};
GN OrderedLocusNames=Adeh_1015 {ECO:0000313|EMBL:ABC80790.1};
OS Anaeromyxobacter dehalogenans (strain 2CP-C).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC80790.1, ECO:0000313|Proteomes:UP000001935};
RN [1] {ECO:0000313|Proteomes:UP000001935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA Zhulin I.B., Loeffler F.E., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP000251; ABC80790.1; -; Genomic_DNA.
DR RefSeq; WP_011420073.1; NC_007760.1.
DR AlphaFoldDB; Q2IPR2; -.
DR STRING; 290397.Adeh_1015; -.
DR KEGG; ade:Adeh_1015; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_3_7; -.
DR OMA; EFGQWAQ; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000001935; 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; cd02004; TPP_BZL_OCoD_HPCL; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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:UP000001935};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 234..362
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 423..572
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 586 AA; 62020 MW; 39D77C7222A18EF7 CRC64;
MADARNGGAV IAAALQRAGV GHLFTLCGGH ISPILVECKR LGLRVVDVRD EANAVFAADA
MARLTGRPGV AAVTAGPGVT NAVTALENAR LAQSPVVLLG GATATLLRGR GALQDIDQLA
LMRPIAKWAT RVTTVGALRP TLERALALAQ GGVPGPVFVE VPVDLLYDEA LVRDLYRRES
GADRVGGVAG TAMRLYLEAH LARQFRAPAL PSLEGLPARI AERIDLRRGT SGGVERIAAR
LSRAERPVLI LGSQALAGCQ DPGRLAASVR ALGVPVYLGG MARGLLGRRD ALQFRHARGR
ALKEADVVVV AGFPFDFRLG YGRGFGRGAF IGAANLSAAE LRKNRSPDVS VEMHPGEFLV
ALAAKAGKPQ AREAWFGALR EREAARDREI AAGAEAAGEL VNPLRFLLRL EEKMAEDAAL
VVDGGDFVAT AAYTLRPRAP LAWLDPGVFG TLGVGGGFAT AAALARPGRE VWLLYGDGSC
AYSLAEFDTF ARHGLAPIAV VGNDGSWQQI AREQVDMLGD DVGTVLARCD YHRVAEGYGG
VGLLLTRDDR IDETLDRARE TARAGRPVCI NVHLRRSEFR KGSISM
//