ID L0I7B0_HALRX Unreviewed; 552 AA.
AC L0I7B0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Thiamine pyrophosphate-dependent enzyme, possible carboligase or decarboxylase {ECO:0000313|EMBL:AGB14673.1};
GN OrderedLocusNames=Halru_0018 {ECO:0000313|EMBL:AGB14673.1};
OS Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halovivax.
OX NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB14673.1, ECO:0000313|Proteomes:UP000010846};
RN [1] {ECO:0000313|Proteomes:UP000010846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18193 / JCM 13892 / XH-70
RC {ECO:0000313|Proteomes:UP000010846};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Halovivax ruber XH-70.";
RL Submitted (SEP-2011) 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; CP003050; AGB14673.1; -; Genomic_DNA.
DR AlphaFoldDB; L0I7B0; -.
DR STRING; 797302.Halru_0018; -.
DR KEGG; hru:Halru_0018; -.
DR eggNOG; arCOG01998; Archaea.
DR HOGENOM; CLU_013748_3_1_2; -.
DR OrthoDB; 6837at2157; -.
DR Proteomes; UP000010846; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:AGB14673.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010846};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..111
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 187..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..537
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 552 AA; 57053 MW; A1C2652B06FCBF64 CRC64;
MRVSTAVVDR LAESGIEAVF GIPGKQTLPL NEAIGGRDDV RFVMARHETA VSHQAWGYAE
TSGKTAATVV VPGPGDMNAM NGLKNAYNDC TPLVHIAVET EPEIRGGEGI HETPPDTYDN
VVKENVLVER PEGAVAALEE AIAIAETAPT GPVRVGIPKN FLGKDVAVAE PPEFSRDGPS
GAAEGDVAAA ADLLADADEP VVIAGGGVRS ADASVDLEAV ATRLDAPVVT TYKGKGTIPA
DHPLSAGTLS GSAPPALLSL LAEADAALAV GTNFDAVATR AWSVDVPDEL VHVTLDPDDL
GTGYEPAVSL LADAADALPA IGEALAERDV AGPTGADETP GSDRAAAVRD DFAERIAELQ
VTDIPLTSVA ALETVRDALP RDTVVAADAG GFRVWGLNAF PAYGPRSYVN PGSWATMGTG
LPSGIGAQVA NPDDDVVVLT GDGGFMMCIH EIHTAVAEDL PLTIVVFRNE DYAIISEEAE
RSYALAESAY GWPDAPIDFV AMAESMGMTA RRAEGRNAVA EAVTEAVSAD EPVLVEVPTD
PHEPQASEWL AE
//
