ID L0IDW9_HALRX Unreviewed; 287 AA.
AC L0IDW9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family {ECO:0000313|EMBL:AGB16406.1};
GN OrderedLocusNames=Halru_1807 {ECO:0000313|EMBL:AGB16406.1};
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:AGB16406.1, 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP003050; AGB16406.1; -; Genomic_DNA.
DR RefSeq; WP_007704616.1; NC_019964.1.
DR AlphaFoldDB; L0IDW9; -.
DR STRING; 797302.Halru_1807; -.
DR GeneID; 14377331; -.
DR KEGG; hru:Halru_1807; -.
DR eggNOG; arCOG01599; Archaea.
DR HOGENOM; CLU_048564_0_0_2; -.
DR OrthoDB; 30755at2157; -.
DR Proteomes; UP000010846; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; cd03375; TPP_OGFOR; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR011896; OFOB.
DR InterPro; IPR032686; PFO_beta_C.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR02177; PorB_KorB; 1.
DR PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR Pfam; PF12367; PFO_beta_C; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:AGB16406.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010846}.
FT DOMAIN 51..198
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 202..261
FT /note="Pyruvate ferredoxin oxidoreductase beta subunit C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12367"
FT REGION 130..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 287 AA; 31096 MW; FCDEC1AF46505F62 CRC64;
MSSDVRFTDF KSDKQPTWCP GCGDFGTMNG MMKALANTGN DPDNTFVVAG IGCSGKIGTY
MHSYALHGVH GRALPVGAGV KMARPDIEVM VAGGDGDGYS IGSGHFIHAV RRNVDMSYVV
MDNRIYGLTK GQASPTSRSD FETSTTPEGP KQPPVNPLAL ALASGATFIA QSFASDAMRH
TEIVEAAIEH DGFGFVNVFS PCVTFNDVDT YDYFRDTLVD LQEEGHDPND YDDAKDVILD
SDKEYQGVIY QDDESVPYGQ HQNLGANMSE IPDGAPEDAM DLVREFY
//
