ID G0LF50_HALWC Unreviewed; 632 AA.
AC G0LF50;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Pyruvate--ferredoxin oxidoreductase alpha subunit {ECO:0000313|EMBL:CCC41613.1};
DE EC=1.2.7.1 {ECO:0000313|EMBL:CCC41613.1};
GN Name=porA {ECO:0000313|EMBL:CCC41613.1};
GN OrderedLocusNames=Hqrw_3880 {ECO:0000313|EMBL:CCC41613.1};
OS Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=768065 {ECO:0000313|EMBL:CCC41613.1, ECO:0000313|Proteomes:UP000007954};
RN [1] {ECO:0000313|EMBL:CCC41613.1, ECO:0000313|Proteomes:UP000007954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16854 / JCM 12705 / C23
RC {ECO:0000313|Proteomes:UP000007954};
RX PubMed=21701686; DOI=10.1371/journal.pone.0020968;
RA Dyall-Smith M., Pfeiffer F., Klee K., Palm P., Gross K., Schuster S.C.,
RA Rampp M., Oesterhelt D.;
RT "Haloquadratum walsbyi: limited diversity in a global pond.";
RL PLoS ONE 6:E20968-E20968(2011).
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DR EMBL; FR746099; CCC41613.1; -; Genomic_DNA.
DR RefSeq; WP_014556945.1; NC_017459.1.
DR AlphaFoldDB; G0LF50; -.
DR GeneID; 12448756; -.
DR KEGG; hwc:Hqrw_3880; -.
DR HOGENOM; CLU_017038_1_0_2; -.
DR OrthoDB; 31112at2157; -.
DR Proteomes; UP000007954; Chromosome.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
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:CCC41613.1}; Pyruvate {ECO:0000313|EMBL:CCC41613.1}.
FT DOMAIN 15..198
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 234..479
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 509..583
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT REGION 423..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 632 AA; 68944 MW; B5200B4C7621B69A CRC64;
MTDDELIWRI AGGSGDGIAS TSQNFAKALM RAGLHVFTHR HYPSRIRGGH TYTEVRVSAD
SVTSRGDGYN FLLALGDSFA RNPQEDAYYG VEEIKPLSEN LDDLDEGGVI VYDTGLLDPD
DIPNFDERID ANNWHVYDIN LREIAREHGR EVMRNTAGVA ITCAIADIDP GIIKDMMADA
MPDKIFEPNM DVFDDAYETV TSEFDATAPD ISVPTGNHDE EQVLVSGSDA IAYGAIDEGC
RFISGYPMTP WTEVFTIMSQ NLPEIGGVSE QVEDEIAAAA LAIGASHAGV KAMSGSSGGG
FALMSEPLGL AEMTETPVVL IEAMRAGPST GMPTKPEQGD LEHVLYTSQG DSHRVVFAPA
DSEEAYHQTR RAFEIAYEYQ IPSIILYDQK NGGELQNIPA TVFDEEPNPD LGSTLTEAEL
EDASHDPSGK YNRFQHAGEN GVSPRSLPGQ EGGRFLATGN EHMPAGHISE DPDNRVNQVD
RRMEKLEAIR DDLETDGQTR NTQYGPSEAQ YGILTFGSQQ GTVREAIDEL DTEGYHVKML
GVSELAPYPV KEVSSFIESV DEVLVVEMNA SAQFRGLTQK ELGRYGDKLS SLLKYNGNPF
EPAEIVDGFI NSIVEDRTLN GNETKYIPAA SD
//
