ID A0A1H5ZVB6_9EURY Unreviewed; 662 AA.
AC A0A1H5ZVB6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:SEG39376.1};
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:QCC47956.1};
GN ORFNames=DV707_09950 {ECO:0000313|EMBL:QCC47956.1}, SAMN04488133_2163
GN {ECO:0000313|EMBL:SEG39376.1};
OS Halobellus limi.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halobellus.
OX NCBI_TaxID=699433 {ECO:0000313|EMBL:SEG39376.1, ECO:0000313|Proteomes:UP000236740};
RN [1] {ECO:0000313|EMBL:SEG39376.1, ECO:0000313|Proteomes:UP000236740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10331 {ECO:0000313|EMBL:SEG39376.1,
RC ECO:0000313|Proteomes:UP000236740};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCC47956.1, ECO:0000313|Proteomes:UP000296733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10331 {ECO:0000313|EMBL:QCC47956.1,
RC ECO:0000313|Proteomes:UP000296733};
RX PubMed=30975999; DOI=.1038/s41467-019-09390-9;
RA Xiong L., Liu S., Chen S., Xiao Y., Zhu B., Gao Y., Zhang Y., Chen B.,
RA Luo J., Deng Z., Chen X., Wang L., Chen S.;
RT "A new type of DNA phosphorothioation-based antiviral system in archaea.";
RL Nat. Commun. 10:1688-1688(2019).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP031311; QCC47956.1; -; Genomic_DNA.
DR EMBL; FNVN01000002; SEG39376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5ZVB6; -.
DR KEGG; hlm:DV707_09950; -.
DR OrthoDB; 6837at2157; -.
DR Proteomes; UP000236740; Unassembled WGS sequence.
DR Proteomes; UP000296733; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
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 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; cd03467; Rieske; 1.
DR CDD; cd07039; TPP_PYR_POX; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR047211; POXB-like.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR Pfam; PF00355; Rieske; 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; SSF50022; ISP domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000236740};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 16..111
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 662 AA; 71181 MW; 209ABA40F194095C CRC64;
MDADTPTGGP DTDVRWYKAL SHDELPEGRV KAVSCGGETV AVTRYDGEYA ALENDCPHQG
GPLGEGSIEA GCLRCPWHGW DFDPLTGETP GPHDDRVGTY PVEEREDGIY VGFPEEGPHE
RTVSDVIAET LVNWGVRQVW GIVGHSNLGL ADALRREADR GNLSYYGVRH EGAGAFAASA
YGKLTGRPAA CFSIAGPGAT NMLTGLWDAN VDRSPAIALT GQVDSQVLGT GNFQEIDLEA
AYGDVAEFEA TVLPDSRHAE LATRAAKTAI LERGVSHLIF PDEIQTKPAV DVEAGDPEGR
IADRDITPPE DALSDAVELL ETAERPVVVV GHGARFEMDG IVELAERFDC PVLTTFKAKG
QIPDSHPLAA GVLGRSGTPI ASHFMNESDL LAVFGASFSN HTGIAEYKPI IHVDYDAMAL
GKFHGVDVPV WGEIGVTVEE LRERLGDDVD AESQREELAD RWEIWREEKA TRRAGTPERG
VNYATAFDAM SRIVPDDAIV PVDVGNNTYA FGRYFEPAGQ SVLMSGYLGS IGFAFPAALG
AWAATREPES RFSGRPVVSV SSDGGFGQYL SEFTTAVKYG MDLTHVLLND DELGKISKEQ
RTGGWDVWQT DLVNPDFAAF AENCGGHGVR VEGEDSLDDA LEEAIDYDGP ALVEILTDSD
PV
//