GenomeNet

Database: UniProt
Entry: S5XRN0_PARAH
LinkDB: S5XRN0_PARAH
Original site: S5XRN0_PARAH 
ID   S5XRN0_PARAH            Unreviewed;       494 AA.
AC   S5XRN0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Glutamate synthase (NADPH/NADH), small chain {ECO:0000313|EMBL:AGT10054.1};
DE            EC=1.4.1.14 {ECO:0000313|EMBL:AGT10054.1};
GN   ORFNames=JCM7686_3018 {ECO:0000313|EMBL:AGT10054.1};
OS   Paracoccus aminophilus JCM 7686.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT10054.1, ECO:0000313|Proteomes:UP000015480};
RN   [1] {ECO:0000313|EMBL:AGT10054.1, ECO:0000313|Proteomes:UP000015480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT10054.1};
RX   PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA   Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA   Schluter A., Puhler A., Bartosik D.;
RT   "Architecture and functions of a multipartite genome of the methylotrophic
RT   bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT   chromids.";
RL   BMC Genomics 15:124-124(2014).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP006650; AGT10054.1; -; Genomic_DNA.
DR   RefSeq; WP_020951691.1; NC_022041.1.
DR   AlphaFoldDB; S5XRN0; -.
DR   STRING; 1367847.JCM7686_3018; -.
DR   KEGG; pami:JCM7686_3018; -.
DR   PATRIC; fig|1367847.3.peg.3037; -.
DR   eggNOG; COG0493; Bacteria.
DR   HOGENOM; CLU_000422_3_1_5; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000015480; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016040; F:glutamate synthase (NADH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:RHEA.
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; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AGT10054.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015480}.
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;  54268 MW;  DC24D559C5916E59 CRC64;
     MATQRMLKFV TVGRQMPEKR EAADRSQDFH EIYREFAAAK ATEQASRCSQ CGVPYCQSHC
     PLHNNIPDWL RLTAEGRTEE AYLLSQETNT FPEICGRICP QDRLCEGNCV IEQSGHGTVT
     IGAIEKYITD TAWEEGWVRA ITPREERPES IGIIGAGPGG LAAADRLRRL GYQVTVYDRH
     DRAGGLLIYG IPGFKLEKDV VERRNKLLAD GGVEFVLNTN IGEDISFDAI RGRHDAVLIA
     TGVYKTRDLD IDNANARGIV RALDYLTASN RVDLGDEVPD FEDGELNAKG KRVVVIGGGD
     TAMDCVRTAI RQGAQSVKCL YRRDRANMPG SQREVQNAEE EGVEFIWMTA PGAFEGHVTG
     EAATAEERDV DGLYGVAAVR VQKMRLGAPD VTGRQSPELI PGADYHEPAE LVIKALGFEP
     EEIPRLWGVD GLEVTRWGTI KAHFQTHRTS LPGVYAVGDI VRGASLVVWA IRDGREAADS
     IVEYLGSTSR VAAE
//
DBGET integrated database retrieval system