ID A0A1U7MUI9_9MICO Unreviewed; 631 AA.
AC A0A1U7MUI9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:OLT23601.1};
GN ORFNames=BJF81_10785 {ECO:0000313|EMBL:OLT23601.1};
OS Ornithinimicrobium sp. CNJ-824.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Ornithinimicrobium.
OX NCBI_TaxID=1904966 {ECO:0000313|EMBL:OLT23601.1, ECO:0000313|Proteomes:UP000185694};
RN [1] {ECO:0000313|EMBL:OLT23601.1, ECO:0000313|Proteomes:UP000185694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNJ-824 {ECO:0000313|EMBL:OLT23601.1,
RC ECO:0000313|Proteomes:UP000185694};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLT23601.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MKKA01000004; OLT23601.1; -; Genomic_DNA.
DR RefSeq; WP_075956966.1; NZ_MKKA01000004.1.
DR AlphaFoldDB; A0A1U7MUI9; -.
DR STRING; 1904966.BJF81_10785; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000185694; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000185694}.
FT DOMAIN 21..211
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 254..479
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 631 AA; 66784 MW; 2A8E7B0569ED04B5 CRC64;
MSSTQLHHLD RVVIRFAGDS GDGMQLTGDR FTSDTASLGN DLSTLPNFPA EIRAPQGTLP
GVSSFQLHFA NHDIATPGDA PDVLVAMNPA ALRANLADLP RGATVIVNSD EFGRRNLAKV
GYEANPLEDG SLTDAGYHVH ALPLTSMAVE ALADFDLTRK EKERAKNMLA LGLLSWLYSR
DTGGTEAFLR AKFAQAPDVL EANLVALRAG HAYGETTEDF AVRYEVAPAP MAPGTYRTIT
GNQAMALGLV AAAQRAGLRL VLGSYPITPA SDVLHQLSAL KHLGVTTLQA EDEIAAVGMA
LGASFGGALG VTTTSGPGLA LKSETIGLAV STELPLVVVD IQRGGPSTGL PTKTEQADLL
QAMYGRNGES PVAVVAAGSP SDCFDAALES VRIATTYRTP VILLSDGYLG NGSEPWSVPD
VASLPDLTVE KASAPNAVDD AGEPVFHPFL RDEQTLARPW AVPGTPGLEH RIGGIEKADV
TGHISYDPAN HDRMVRLRQA KIDRIADTIP PLAVDDPDGR ARLLVLGWGS TYGPVAAATR
LARSAGASVA RAHLRHLNPF PADLGEVLRR YDRVLLPEMN LGQLALLLRG RFLVDVRSHT
AVRGLPFTAA ELAEVIHAHL LELTEAPEEA R
//
