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Database: UniProt
Entry: M1REZ8_9AQUI
LinkDB: M1REZ8_9AQUI
Original site: M1REZ8_9AQUI 
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
//
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