ID A0A099F2P8_9RHOB Unreviewed; 494 AA.
AC A0A099F2P8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Dihydropyrimidine dehydrogenase {ECO:0000313|EMBL:KGJ04462.1};
DE SubName: Full=Glutamate synthase (NADPH) small subunit {ECO:0000313|EMBL:SFA54341.1};
GN ORFNames=IT41_10095 {ECO:0000313|EMBL:KGJ04462.1}, SAMN04487972_11224
GN {ECO:0000313|EMBL:SFA54341.1};
OS Paracoccus halophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=376733 {ECO:0000313|EMBL:KGJ04462.1, ECO:0000313|Proteomes:UP000029846};
RN [1] {ECO:0000313|EMBL:KGJ04462.1, ECO:0000313|Proteomes:UP000029846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ04462.1,
RC ECO:0000313|Proteomes:UP000029846};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ04462.1, ECO:0000313|Proteomes:UP000029846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ04462.1,
RC ECO:0000313|Proteomes:UP000029846};
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.
RN [3] {ECO:0000313|EMBL:SFA54341.1, ECO:0000313|Proteomes:UP000182312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6117 {ECO:0000313|EMBL:SFA54341.1,
RC ECO:0000313|Proteomes:UP000182312};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JRKN01000011; KGJ04462.1; -; Genomic_DNA.
DR EMBL; FOJO01000012; SFA54341.1; -; Genomic_DNA.
DR RefSeq; WP_036740750.1; NZ_JRKN01000011.1.
DR AlphaFoldDB; A0A099F2P8; -.
DR STRING; 376733.SAMN04487972_11224; -.
DR eggNOG; COG0493; Bacteria.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000029846; Unassembled WGS sequence.
DR Proteomes; UP000182312; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 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; IPR006006; GltD-like.
DR InterPro; IPR009051; Helical_ferredxn.
DR NCBIfam; TIGR01318; gltD_gamma_fam; 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; 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029846}.
FT DOMAIN 26..136
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 152..474
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 494 AA; 54139 MW; 1847EAE059DF6C83 CRC64;
MATQKMLKFV TVGREMPEKR DAASRSEDFH EIYREFAAAK ASEQASRCSQ CGVPYCQTHC
PLHNNIPDWL RLTAEGRTQE AYLRSQETNT FPEICGRICP QDRLCEGNCV IEQSGHGTVT
IGAIEKYITD TAWEEGWVQP IAPLQERPES IGIIGAGPGG LAAADRLRRM GFQVTVYDRH
DRAGGLMIYG IPGFKLEKHV VERRNRQLAD GGVEFVLNAN VGEDISFDAI RGKHDAVLIA
TGVYKTRDLD IDNAEARGVV RALDYLTASN RVDLGDEIPD YEDGELNARG KRVIVIGGGD
TAMDCVRTAI RQGAQSVKCL YRRDRANMPG SQREVQNAEE EGVEFVWLSA PGAFAGHVTG
EAMAAQEVDV DGDPAIASVR VQKMRLGPPD VSGRQSPELI EGADYDEPAD LVIKALGFEP
EDLPRLWGVE GLEVTRWGTI RADYQTHMTS LPGVYAVGDI VRGASLVVWA IRDGREAADS
IANWLVDSAR IAAE
//
