ID F8CG99_MYXFH Unreviewed; 486 AA.
AC F8CG99;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=glutamate synthase (NADPH) {ECO:0000256|ARBA:ARBA00012079};
DE EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
GN OrderedLocusNames=LILAB_27820 {ECO:0000313|EMBL:AEI67451.1};
OS Myxococcus fulvus (strain ATCC BAA-855 / HW-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=483219 {ECO:0000313|EMBL:AEI67451.1, ECO:0000313|Proteomes:UP000000488};
RN [1] {ECO:0000313|EMBL:AEI67451.1, ECO:0000313|Proteomes:UP000000488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-855 / HW-1 {ECO:0000313|Proteomes:UP000000488};
RX PubMed=21868801; DOI=10.1128/JB.05516-11;
RA Li Z.F., Li X., Liu H., Liu X., Han K., Wu Z.H., Hu W., Li F.F., Li Y.Z.;
RT "Genome sequence of the halotolerant marine bacterium Myxococcus fulvus HW-
RT 1.";
RL J. Bacteriol. 193:5015-5016(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine
CC + NADPH; Xref=Rhea:RHEA:15501, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58359; EC=1.4.1.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001895};
CC -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+)
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00037898}.
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DR EMBL; CP002830; AEI67451.1; -; Genomic_DNA.
DR AlphaFoldDB; F8CG99; -.
DR STRING; 483219.LILAB_27820; -.
DR KEGG; mfu:LILAB_27820; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_1_7; -.
DR OMA; DCVGTAH; -.
DR Proteomes; UP000000488; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; 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; 2.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 25..131
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 146..458
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 486 AA; 52265 MW; A9DC753A9F449462 CRC64;
MGKPTGFIEW ERVHADKRDK AERLNDWREF ALPLSADEAR RQAGRCMDCG VPFCHQGCPL
GNLIPDFNEA VYRGRWREAY DLLSRTNGFP EMTGRLCPAP CEAACVLAID QHPVTIEQME
KEIAERAFKE GWVKPRPPAR RTGKTVGVVG SGPAGLAAAA QLNAAGHTVT VYERDARPGG
LLRYGIPDFK LEKAVVDRRV ALMEAEGITF VTGADVGGAV SFQELRAKHD ALVLALGARR
PRELEVPGRE LSGVVQAMAY LEHQNRRVSG HGEKDPRLDA AGRHVVVLGG GDTGSDCLGT
ALRQGAASVR QVELLPAPPA VRAEGNPWPR WPVIFRTSTS QEEGGDRHFA LMTKRLTGSD
GRLEALHAVE VELQREPGAL PRIVERPGSE VTFQADLLVL AMGFTGPETA NLSEALGVKL
SPRGTVQVDA RFATSADGVF CAGDASRGAS LIVWALSDGR EAAKACDAYL TGGRSALPTR
GADCAF
//