ID A0A099GHW0_9RHOB Unreviewed; 519 AA.
AC A0A099GHW0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Dihydropyrimidine dehydrogenase {ECO:0000313|EMBL:KGJ22147.1};
GN ORFNames=IX56_09915 {ECO:0000313|EMBL:KGJ22147.1};
OS Paracoccus sanguinis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1545044 {ECO:0000313|EMBL:KGJ22147.1, ECO:0000313|Proteomes:UP000029858};
RN [1] {ECO:0000313|EMBL:KGJ22147.1, ECO:0000313|Proteomes:UP000029858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5503 {ECO:0000313|EMBL:KGJ22147.1,
RC ECO:0000313|Proteomes:UP000029858};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ22147.1, ECO:0000313|Proteomes:UP000029858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5503 {ECO:0000313|EMBL:KGJ22147.1,
RC ECO:0000313|Proteomes:UP000029858};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:KGJ22147.1}.
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DR EMBL; JRKQ01000046; KGJ22147.1; -; Genomic_DNA.
DR RefSeq; WP_036709748.1; NZ_JRKQ01000046.1.
DR AlphaFoldDB; A0A099GHW0; -.
DR Proteomes; UP000029858; Unassembled WGS sequence.
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; 3.
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; 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; 2.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029858}.
FT DOMAIN 25..136
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 151..399
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 429..499
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 519 AA; 56098 MW; 5265C016D2695D8A CRC64;
MATQTMLKFV TVPRQMPDKR TAAERAEDFH EIYREFADAK AKEQASRCSQ CGVPYCQSHC
PLHNNIPDWL RLTAEGRTQE AYLRAQETNS FPEICGRICP QDRLCEGNCV IEQSGHGTVT
IGAIEKYITD TAWDEGWVQP IRPAAERAES VGIIGAGPGG LAAADRLRRM GFQVTVYDRH
DRAGGLLIYG IPGFKLEKPV VERRNRLLEE GGVEFVLGAD VGQTISFDAI RGKHDAVLIA
TGVYQTRDLD IDNAPERGVV RALDYLTASN RVDLGDEVPD FEDGELNAAG KRVVVIGGGD
TAMDCVRTAI RQGATSVKCL YRRDRANMPG SQREVQNAEE EGVEFVWLSA PNAFAGHAPG
VARKADEGAV ANAGGDLSGD GVGDNPTLAP AHVPVETPSR VNGLRVTRMR LGAPDVSGRQ
SPEPIEGADY DEPADLVIKA LGFEPEDIPR LWGVEGLEVT RWGTIKADFR THRTSLPGVW
AVGDIVRGAS LVVWAIRDGR EAADAIAAEL AGASRLAAE
//
