ID M1REZ8_9AQUI Unreviewed; 607 AA.
AC M1REZ8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein {ECO:0000313|EMBL:AGG15726.1};
GN ORFNames=HydHO_1417 {ECO:0000313|EMBL:AGG15726.1};
OS Hydrogenobaculum sp. HO.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC Hydrogenobaculum.
OX NCBI_TaxID=547144 {ECO:0000313|EMBL:AGG15726.1, ECO:0000313|Proteomes:UP000011725};
RN [1] {ECO:0000313|EMBL:AGG15726.1, ECO:0000313|Proteomes:UP000011725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HO {ECO:0000313|EMBL:AGG15726.1,
RC ECO:0000313|Proteomes:UP000011725};
RX PubMed=23435891; DOI=10.1128/AEM.03591-12;
RA Romano C., D'Imperio S., Woyke T., Mavromatis K., Lasken R., Shock E.L.,
RA McDermott T.R.;
RT "Comparative Genomic Analysis of Phylogenetically Closely Related
RT Hydrogenobaculum sp. Isolates from Yellowstone National Park.";
RL Appl. Environ. Microbiol. 79:2932-2943(2013).
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DR EMBL; CP004347; AGG15726.1; -; Genomic_DNA.
DR RefSeq; WP_015419993.1; NC_020411.1.
DR AlphaFoldDB; M1REZ8; -.
DR STRING; 547144.HydHO_1417; -.
DR KEGG; hho:HydHO_1417; -.
DR PATRIC; fig|547144.3.peg.1436; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR HOGENOM; CLU_017038_1_0_0; -.
DR Proteomes; UP000011725; Chromosome.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
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 Pyruvate {ECO:0000313|EMBL:AGG15726.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011725}.
FT DOMAIN 13..174
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 210..385
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 482..554
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 607 AA; 67483 MW; 0B4836CDBAE0834B CRC64;
MAFSLVIKIG GEGGEGVISA GDFLTEAAVR SGYHVVNFKS FPAEIKGGYA NSTVRISDEK
LYSTGDGFDI LCCFNAEAYA YNKKHLKPGT VLVYDSSDFE PEEHEGVIMY PVPLSDIAKN
QIKAYITKNI VALGALTGLF NLPVESLKDS IKAKFSRKGE KIVSMNYQAL EAGINYVKEN
LVKKDGFEFP PPIGLKDVVI MEGNQAVAKG CVAAGCQFYA AYPITPATSV GNYIVEDLIR
KDGWLYQAED EIASLAMAIG ASFAGAKAMT ATSGPGLSLM SELIGYAGMT ETPVVIVDVQ
RVGPATGMPT KHEQGDLYHA VYGSHGEIPR AVLAPISVED SFYMSVEAFN LAEKYQMPVI
MLTDAAMSLR AEAFPTPDLS KLNIVNRLIY NSEEDKEQKF IRHGRFLRYA LFTEDGITPM
GIPGDPNAIH AITGLERQEN SDPRNRPDIR TYQMNKRFKK LEKLLEEDYD RFIEIDAPYK
DADIGIITWG LTASITKEAV QRLRSRGLKI NAMYPRLLWP VKEDVFEFFA KSSKRILIPE
TNYYGQLATI VKDRTHIRPI SYNIYRGEPF IPKEIEDIVD FLMENQEITE GRFTPEHIYG
EKAYGLI
//