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
//