ID W0ESQ3_9BACT Unreviewed; 493 AA.
AC W0ESQ3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Dihydropyrimidine dehydrogenase subunit A {ECO:0000313|EMBL:AHF12199.1};
GN ORFNames=BARVI_04725 {ECO:0000313|EMBL:AHF12199.1};
OS Barnesiella viscericola DSM 18177.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae;
OC Barnesiella.
OX NCBI_TaxID=880074 {ECO:0000313|EMBL:AHF12199.1, ECO:0000313|Proteomes:UP000018901};
RN [1] {ECO:0000313|EMBL:AHF12199.1, ECO:0000313|Proteomes:UP000018901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18177 {ECO:0000313|Proteomes:UP000018901};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP007034; AHF12199.1; -; Genomic_DNA.
DR RefSeq; WP_025278096.1; NZ_CP007034.1.
DR AlphaFoldDB; W0ESQ3; -.
DR STRING; 880074.BARVI_04725; -.
DR KEGG; bvs:BARVI_04725; -.
DR PATRIC; fig|880074.11.peg.996; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_3_10; -.
DR Proteomes; UP000018901; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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 InterPro; IPR006004; SudA-like.
DR NCBIfam; TIGR01316; gltA; 1.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 44..154
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 169..475
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 493 AA; 54079 MW; F20502403FD41CA2 CRC64;
MNKEELAAQR AEQWREELRK SKKAKERTDI PRVKMKELDP AYRVTNREEV NCGLTPEQAV
LEATRCLDCV EPLCMTGCPV GINIPKFIKN IERGDFREAA RTLKETSALP AVCGRVCPQE
RQCESKCFYL QKLKKEPIAI GYLERFAADY EQASGEVALP DMKPDNGIKI AVVGSGPCGL
SFAGDMAKLG YRVTVFEALH EIGGVLKYGI PEFRLPNRIV DVEIDSLRRM GVEFMTDCIV
GKTLSYDDLH EMGFKGIMVA SGAGLPRFMN IPGENLNGVM SSNEYLTRVN LMDAANPESD
TPVYKGHRVA VIGGGNTAMD SVRTARRLGA DRAMIVYRRS EAEMPARQEE VHHAKQEGVE
FLTLHNPIEY IGDERGRVRQ MKLQKMELGE PDASGRRSPV PIPGAIETID VDEVIVSVGV
SPNPLVPNAI EGLEVTPKGT IVVNADTLQS ALPDIYAGGD IVRGGATVIL AMGDGRRAAA
AMHEALQKQQ RSA
//
