ID D3UYT4_XENBS Unreviewed; 1122 AA.
AC D3UYT4;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Putative oxyreductase protein {ECO:0000313|EMBL:CBJ79462.1};
DE EC=1.2.7.8 {ECO:0000313|EMBL:CBJ79462.1};
GN OrderedLocusNames=XBJ1_0312 {ECO:0000313|EMBL:CBJ79462.1};
OS Xenorhabdus bovienii (strain SS-2004).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79462.1, ECO:0000313|Proteomes:UP000002045};
RN [1] {ECO:0000313|EMBL:CBJ79462.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79462.1};
RX PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA Goodrich-Blair H.;
RT "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT convergent lifestyles from divergent genomes.";
RL PLoS ONE 6:E27909-E27909(2011).
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DR EMBL; FN667741; CBJ79462.1; -; Genomic_DNA.
DR RefSeq; WP_012986922.1; NC_013892.1.
DR AlphaFoldDB; D3UYT4; -.
DR STRING; 406818.XBJ1_0312; -.
DR KEGG; xbo:XBJ1_0312; -.
DR PATRIC; fig|406818.4.peg.284; -.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG4231; Bacteria.
DR HOGENOM; CLU_009166_1_0_6; -.
DR Proteomes; UP000002045; Chromosome.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR046667; DUF6537.
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 PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR Pfam; PF20169; DUF6537; 1.
DR Pfam; PF01558; POR; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CBJ79462.1}.
FT DOMAIN 709..892
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 918..1116
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1122 AA; 124447 MW; 95F4FEBFB3C4D09D CRC64;
MTQHYPSKFV TGTDALAELL LAQAELDKSH NLNTAGFVAG YRGSPLARLD QALWQHGKEL
AQSNIRFQPA INEDLAATAL IGTQKVESDP DRNVIGVFGM WYGKGPGVDR SGDALRHGNA
YGSSPHGGVL VILGDDHGCV SSSMSHQSDL VLMAWSMPIL HPASVSDYHD VGLWGWAASR
ASGAWVGFKA ISEVVESSAI RKSKPFPEYK TPEIDSGPDG LHWRWPDLPG PQIEKRLAYK
LKAVEAFARA NPIDQLLAPC AHPRALLVTV GKAHRDVLEA LRAGGLTPSQ LAKQGVAFVH
VRLVYPLSPL LSDLASQVTD IFVIEEKNAV VEILLARHLV NSQKNIKLIG KHNHLGQQFL
PADIELRPSL ITPLLSGWLN KLDLFLSVPL EWATKTTPHD LTLPKRTPYF CAGCPHSTST
RLPEGSQAQI GIGCHVMAAW MDRNTGFGLV QMGGEGADWV GHSPFINRPH LFQNLGDGTY
FHSGHLSIRQ SIAAGNHITY KLLFNQAVAM TGGQPLDGNL TIPQIVALML AEGVKEVAIV
TDDIDKYQDK NLLTAKVTLY QRDYLEEVQK RFREIAGVTV IIYDQACATE LRRKRKRGLE
PKATRRAVIN ELVCEGCGDC QVQSNCLAVI PVKTSLGTKR KIDQHVCNSD LSCLKGFCPS
FVTVENANPR HDLSKIIPQG DLDKLLRELP QPILIISDNP YEILLVGVGG TGIVTAGNLL
AIAAEADNYS VSLLNFTGFA QKGGEAITHV RLCHDMNKLH QVRIDRGRAN LIIAADLVAA
TGQNSLTVMS KSATKCVLNT HETQIGTMLR APTLNLDHPK MMTTLHQHCQ TLNSIDAEIM
AADLVGDRNQ TNIVLIGYAW QLGKIPITLS AIDHTIQALG NAADSARRAF HIGRIAAVQP
DILNERLHIK PQESIKTLDD LIMHRYQFLV DYQNEGYAQR YLSRVAQIQL VTQQIDAEEI
AKAVAENLFK LMAYKDEYEV ARLYAKSDFF ENLRSQFDNT DNIRFHFSLP LFNRKDPRTG
ERGKREYGTW IIPIFRVLAA CKPLRGTMFD IFGYQEERRQ ERNLLLEYER LLDFLIEKLN
RDNLAICQQL AELPDQVRGF GHVKQKAIKN MMERKEALLE KL
//
