ID A0A0K2G835_NITMO Unreviewed; 444 AA.
AC A0A0K2G835;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Pyruvate:ferredoxin oxidoreductase alpha subunit {ECO:0000313|EMBL:ALA57118.1};
DE EC=1.2.7.3 {ECO:0000313|EMBL:ALA57118.1};
GN Name=forA {ECO:0000313|EMBL:ALA57118.1};
GN ORFNames=NITMOv2_0682 {ECO:0000313|EMBL:ALA57118.1};
OS Nitrospira moscoviensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA57118.1, ECO:0000313|Proteomes:UP000069205};
RN [1] {ECO:0000313|EMBL:ALA57118.1, ECO:0000313|Proteomes:UP000069205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA57118.1,
RC ECO:0000313|Proteomes:UP000069205};
RX PubMed=26305944; DOI=10.1073/pnas.1506533112;
RA Koch H., Lucker S., Albertsen M., Kitzinger K., Herbold C., Spieck E.,
RA Nielsen P.H., Wagner M., Daims H.;
RT "Expanded metabolic versatility of ubiquitous nitrite-oxidizing bacteria
RT from the genus Nitrospira.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11371-11376(2015).
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DR EMBL; CP011801; ALA57118.1; -; Genomic_DNA.
DR RefSeq; WP_053378510.1; NZ_CP011801.1.
DR AlphaFoldDB; A0A0K2G835; -.
DR STRING; 42253.NITMOv2_0682; -.
DR KEGG; nmv:NITMOv2_0682; -.
DR PATRIC; fig|42253.5.peg.676; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000069205; Chromosome.
DR GO; GO:0047553; F:2-oxoglutarate 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 InterPro; IPR033412; PFOR_II.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01855; POR_N; 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:0000313|EMBL:ALA57118.1};
KW Pyruvate {ECO:0000313|EMBL:ALA57118.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000069205}.
FT DOMAIN 64..283
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 308..402
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 48411 MW; 84246F84C5BFDE71 CRC64;
MSETEVKTNP QGDPITSVAV PKSDGKKDPH AEAKKQRVVT PEYMFHEAPR TKEFITGSEA
AKEAIRRSNV DLAIAYPITP QSETMQLVGV LYGEGYVKEY YRGEEEVGVM AAIAGGSRSG
VRCFTATAGP GTLRGLEGIA SWPGHRLPVV AMFTCRVVNA PLAIQPDNIE VAYLINCGMI
VFHAENQQDM FDFIMAGFTI SEKNDVTLPV GVCCDGFFVT HARGYVRMQD RGIKLPPREA
WRGAVPVLDA ENPPARLSRD APVQKSNFMA YNIHAVWQQE VWAAVERSRK YINRYMGGLL
TAENVDDAEA IIIASGSAAA QSREAVRLCA EKGIKVGLIK IRSLRPFPTQ ELRALCGKAK
LIVVPEFNYV GWLAKEVATA IYGYSKAKII GGPRVYGGQS MPVELIVDEV ESGLTGKKST
NVALSSIMGG QVNPDEVAHF MRSI
//
