ID A9WEY2_CHLAA Unreviewed; 844 AA.
AC A9WEY2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Thiamine pyrophosphate protein central region {ECO:0000313|EMBL:ABY35297.1};
GN OrderedLocusNames=Caur_2085 {ECO:0000313|EMBL:ABY35297.1};
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY35297.1, ECO:0000313|Proteomes:UP000002008};
RN [1] {ECO:0000313|Proteomes:UP000002008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl
RC {ECO:0000313|Proteomes:UP000002008};
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
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; CP000909; ABY35297.1; -; Genomic_DNA.
DR RefSeq; WP_012257951.1; NC_010175.1.
DR RefSeq; YP_001635686.1; NC_010175.1.
DR AlphaFoldDB; A9WEY2; -.
DR STRING; 324602.Caur_2085; -.
DR EnsemblBacteria; ABY35297; ABY35297; Caur_2085.
DR KEGG; cau:Caur_2085; -.
DR PATRIC; fig|324602.8.peg.2365; -.
DR eggNOG; COG0028; Bacteria.
DR eggNOG; COG4221; Bacteria.
DR HOGENOM; CLU_017084_0_0_0; -.
DR InParanoid; A9WEY2; -.
DR Proteomes; UP000002008; Chromosome.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR CDD; cd05374; 17beta-HSD-like_SDR_c; 1.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
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; 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; PF00106; adh_short; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002008};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 295..408
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 483..610
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 677..825
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 844 AA; 90486 MW; 082B1270AF102A2D CRC64;
MTATISRRVW LITGAGGGFG RSLVRQLLER GEYVAAADRS LELLAALPSS EDGCLFPVAI
DLTDPMTIQA GVAAVIDRFG RIDVLVNNAG LGHGGPLEEV SLTDIRRLFD VNIIGMMLIT
QAVLPVMRAA GGGRIINLSS DSGVIGFPFQ GLYTATKHAV EGFSDSLYQE VAPFGIHVSV
VQPCGMFKTA MPANAIAQAR SALKPDSPYA DRVLRMASAL SAAWETARDP AEVAQAILDV
ADADPPPIRR RVGAPERTGL LGLRQQMSHD DLVRFIYRLT AEPTPPPLPK VRGDGGWLVV
RTLREAGITH AFTIVGGHNY QIVNACREEG LCVIDARNEM HAAHMADAFA RLARRPALLT
VDAAPGLVNA VAGIEVAYEA QVPMIVVSAQ GSLAGRDIGV MQAIDQLRLV RPITKWQRTC
FETRRLPEYT AAAIRHATTG RPGPTFLDFP LEVMQATIDV ETVPQPRHYR VTSGPLADPD
LLRQVIEMLR KARRPLIIAG SGVWWAHGEA ELVRFVQTTG IPVLTRNLAR GIIPDDHPLA
AGFYPSPAAL ADAFLVIGTR LDWTIGYGRP PLFSPDAPVA QIDLHPESIG KTRPIEIGIV
ADAAQALRQL NAMVSATGPW TMDAEWPALA HGSIAAMRQQ TAAAAQLSTR DQRPIHSIEL
MQALAECLPR EAIKVVDGGY SAAFAIQYLD AYVPSGVLWV GSTGHLGVGL GFAIGAKRAR
PDAPVVAIMG DGAFGLCGME FDTAVRHQLP IVVVVANDAG WGETRDGQRR RWGDAAIVGT
ALNPTRYDEL ARALGGHGEY VTRLDELAPA IRRAFAAGKP ALINVITDPE QRSSAVSGLP
WIVE
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