ID F7PID4_9EURY Unreviewed; 631 AA.
AC F7PID4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=2-oxoglutarate oxidoreductase, alpha subunit {ECO:0000313|EMBL:CCQ34855.1};
DE SubName: Full=Putative 2-ketoglutarate ferredoxin oxidoreductase protein {ECO:0000313|EMBL:ERJ04739.1};
DE EC=1.2.7.3 {ECO:0000313|EMBL:CCQ34855.1, ECO:0000313|EMBL:ERJ04739.1};
GN Name=korA {ECO:0000313|EMBL:ERJ04739.1};
GN ORFNames=HLRTI_003300 {ECO:0000313|EMBL:ERJ04739.1}, HTIA_2753
GN {ECO:0000313|EMBL:CCQ34855.1};
OS Halorhabdus tiamatea SARL4B.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorhabdus.
OX NCBI_TaxID=1033806 {ECO:0000313|EMBL:ERJ04739.1, ECO:0000313|Proteomes:UP000003861};
RN [1] {ECO:0000313|EMBL:ERJ04739.1, ECO:0000313|Proteomes:UP000003861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ04739.1,
RC ECO:0000313|Proteomes:UP000003861};
RX PubMed=21705593; DOI=10.1128/JB.05462-11;
RA Antunes A., Alam I., Bajic V.B., Stingl U.;
RT "Genome sequence of Halorhabdus tiamatea, the first archaeon isolated from
RT a deep-sea anoxic brine lake.";
RL J. Bacteriol. 193:4553-4554(2011).
RN [2] {ECO:0000313|EMBL:ERJ04739.1, ECO:0000313|Proteomes:UP000003861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|EMBL:ERJ04739.1,
RC ECO:0000313|Proteomes:UP000003861};
RX PubMed=24324765;
RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA Bajic V.B.;
RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT the Red Sea Extremophiles.";
RL PLoS ONE 8:E82210-E82210(2013).
RN [3] {ECO:0000313|EMBL:CCQ34855.1, ECO:0000313|Proteomes:UP000015381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|Proteomes:UP000015381}, and Type strain:
RC SARL4B {ECO:0000313|EMBL:CCQ34855.1};
RX PubMed=24428220; DOI=10.1111/1462-2920.12393;
RA Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S.,
RA Ciordia S., Albar J.P., Alcaide M., La Cono V., Yakimov M.M., Antunes A.,
RA Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O., Golyshina O.V.,
RA Golyshin P.N., Teeling H.;
RT "Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements
RT identify the first cultivated euryarchaeon from a deep-sea anoxic brine
RT lake as potential polysaccharide degrader.";
RL Environ. Microbiol. 16:2525-2537(2014).
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DR EMBL; HF571520; CCQ34855.1; -; Genomic_DNA.
DR EMBL; AFNT02000059; ERJ04739.1; -; Genomic_DNA.
DR RefSeq; WP_008525361.1; NZ_AFNT02000059.1.
DR STRING; 1033806.HTIA_2753; -.
DR GeneID; 23798700; -.
DR KEGG; hti:HTIA_2753; -.
DR PATRIC; fig|1033806.12.peg.2740; -.
DR eggNOG; arCOG01606; Archaea.
DR HOGENOM; CLU_017038_1_0_2; -.
DR OrthoDB; 31112at2157; -.
DR Proteomes; UP000003861; Unassembled WGS sequence.
DR Proteomes; UP000015381; Chromosome.
DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC.
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; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR NCBIfam; TIGR03710; OAFO_sf; 1.
DR PANTHER; PTHR32154:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ERJ04739.1}.
FT DOMAIN 15..200
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 234..475
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 508..581
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT REGION 434..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 68957 MW; BD1EFFDF393F4625 CRC64;
MTDNELIWRI AGGSGDGIAS TSQNFAKALM RAGLNIFTHR HYPSRIRGGH TYVEVRAKDE
EVTSRGDGYN FLLSLGDSFA RNPAEDAYYG NEERKPLAEN LDELREGGVI VYDTGLFDED
EVAELNLEER AAENDWHVYP VNLREIAREH GRDVMRNTAG VGITAALLGM DVSYFEELIT
QNMSGDIQED NLNVLADAYE QAQDFEFTHD LEVPTGDNET EMALMNGSQS IAYGAFDEGC
RFISGYPMTP WTEVFTIMSQ HMSEFGGVAE QVEDEIAAAA MALGASHAGV KAMSGSSGGG
FALMSEPLGL AEMTETPIVL VEAMRAGPST GMPTKPEQGD LEHVLYTSQG DSARVVFAPA
GVKEAYEQTR TAFEIAYDYQ IPAIVVYDQK IEGELRSVPV EFFDREPDAD LGKVLSEAEI
KEAAHHEAGA FQRFDPNAED GVSPRTVPGQ KGGRHLTSGN ETNDYGHIDE DPDNRVAHMS
RRIGKLDTIR EDLDAGETNQ AYRGPEDAEY GIVTWGSQQG TVFEAVDRLN DEGHSVKAIG
VSDLMPYPEA EMTEFLESVE EAIVVEMNAS GQFKGLTQKE LGRFGDKLSS LLKYNGNPFE
PAEIVEGFEA IVENEPDIPG NSTTFVPAAG D
//
