ID Q5E1C6_ALIF1 Unreviewed; 598 AA.
AC Q5E1C6;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Predicted oxidoreductase {ECO:0000313|EMBL:AAW87170.1};
DE EC=1.2.1.43 {ECO:0000313|EMBL:AAW87170.1};
GN Name=yeiT {ECO:0000313|EMBL:AAW87170.1};
GN OrderedLocusNames=VF_A0100 {ECO:0000313|EMBL:AAW87170.1};
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309 {ECO:0000313|EMBL:AAW87170.1, ECO:0000313|Proteomes:UP000000537};
RN [1] {ECO:0000313|EMBL:AAW87170.1, ECO:0000313|Proteomes:UP000000537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114 {ECO:0000313|Proteomes:UP000000537};
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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DR EMBL; CP000021; AAW87170.1; -; Genomic_DNA.
DR RefSeq; WP_011263001.1; NC_006841.2.
DR RefSeq; YP_206058.1; NC_006841.2.
DR AlphaFoldDB; Q5E1C6; -.
DR STRING; 312309.VF_A0100; -.
DR EnsemblBacteria; AAW87170; AAW87170; VF_A0100.
DR KEGG; vfi:VF_A0100; -.
DR PATRIC; fig|312309.11.peg.2704; -.
DR eggNOG; COG0247; Bacteria.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_4_6; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000000537; Chromosome II.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 2.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF13534; Fer4_17; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 2.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:AAW87170.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000537}.
FT DOMAIN 19..106
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 120..403
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 598 AA; 65793 MW; CAA2D97078241064 CRC64;
MSNVIFSQKL YDTAQMVVDG CMGDADPACQ TACPMHTDVK QYVRLAGEGN YQEALDLIRG
KLFLPQTLGR ICAHPCEAAC RRNTEYNQPI SVAGIKRFVA EKMDKQSNWD LTVANDSGKK
IAIVGAGPAG AQAAIELRRS GHQVTIYEKL NVYGGMMRVG IPEYRLPRDV IDFEYGYLDM
LGIETKFGIE IGKDISFNEL RLSHDAIILA HGAHVGSIIP LPGHKAQGVF SAVEYLKEVS
ETRDFPRAGK RIMVIGGGDV AMDCARSSWR IGVDEVHQCS LEEMAKLPAS QIEIDESLEE
GVLFNAGWGP ISIEETDGKV TGIVLKKVIS IFDENGNFSP SYSDETRTIA VDTVIFATGQ
VVADITDGAL EQTRGGRYVV DKDTLASSVD GVYVAGDACG GNIVVEAMAL GHKAALSIER
QFAKRPLTEN RDFEKEYNYP SRLDIPLPKG TTDTPRLHGQ LRDAEERKQD FKQVDLGFSE
EQIKQEASRC LQCTCKLCMN ECVMMNDFGD CPKTLFSDFI NNKTMDPLLA YSCNACDQCT
IVCPKDYPMK EMFLSARVDF VNANGGNSPI PGHKAINMHQ KLGFSKFFTM AKRTVASK
//
