ID F2JNM6_CELLD Unreviewed; 495 AA.
AC F2JNM6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Glutamate synthase, NADH/NADPH, small subunit {ECO:0000313|EMBL:ADZ85915.1};
DE EC=1.4.1.14 {ECO:0000313|EMBL:ADZ85915.1};
GN OrderedLocusNames=Clole_4243 {ECO:0000313|EMBL:ADZ85915.1};
OS Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS RHM5) (Clostridium lentocellum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC Cellulosilyticum.
OX NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ85915.1, ECO:0000313|Proteomes:UP000008467};
RN [1] {ECO:0000313|EMBL:ADZ85915.1, ECO:0000313|Proteomes:UP000008467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC {ECO:0000313|Proteomes:UP000008467};
RX PubMed=21398547; DOI=10.1128/JB.00239-11;
RG US DOE Joint Genome Institute;
RA Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA Angert E.R., Currie C.R.;
RT "Complete genome sequence of the cellulose-degrading bacterium
RT Cellulosilyticum lentocellum.";
RL J. Bacteriol. 193:2357-2358(2011).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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; CP002582; ADZ85915.1; -; Genomic_DNA.
DR RefSeq; WP_013659185.1; NC_015275.1.
DR AlphaFoldDB; F2JNM6; -.
DR STRING; 642492.Clole_4243; -.
DR KEGG; cle:Clole_4243; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_1_9; -.
DR Proteomes; UP000008467; Chromosome.
DR GO; GO:0016040; F:glutamate synthase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:RHEA.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0006537; P:glutamate biosynthetic process; 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; IPR006005; Glut_synth_ssu1.
DR InterPro; IPR009051; Helical_ferredxn.
DR NCBIfam; TIGR01317; GOGAT_sm_gam; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ADZ85915.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008467}.
FT DOMAIN 23..139
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 154..477
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 495 AA; 54508 MW; 80F43AAC6766A5E1 CRC64;
MGKPTGFMEY DRTTSRSIAP AQRVKNFKEF HIPLAKEKQE VQGARCMDCG VPFCQSGIML
KGATSGCPLN NLIPEWNDLI FNGQWEEAAR RLLLTNNFPE FTGRVCPAPC ENACTCSLNG
DAVAIKENEE AIIENAFAKG LIKPKKPSVR TGKNVAIVGS GPAGLAAAAQ LNKRGHTVTV
YERSDRVGGL LMYGIPNMKI EKHIIERRVD LMVQEGIKFI TNADIGRKYK ANKLLKEYDA
VILACGASNP RDINAPGRDA KGIYFAVDFL KSTTMSLLNS NLEDGTYMSA KGKNVVVIGG
GDTGNDCVGT SIRHGCKSVV QIEMMPKLPD QRADNNPWPQ WARVCKTDYG QEEAIETFGS
DPRIYETTVK EFCKDENGDL VGVKVVKVKF VTNEETGRRE MREVEGSEQL LDADLVLIAA
GFLGSENYVT DSFGVDVDAR TNVTTELGEY KTNIEKVFTA GDMHRGQSLV VWAIREGREA
AKEVDEYLMG YTNLR
//
