ID A0A1I6KER9_9BURK Unreviewed; 491 AA.
AC A0A1I6KER9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glutamate synthase (NADH) small subunit {ECO:0000313|EMBL:SFR89731.1};
GN ORFNames=SAMN05428960_2862 {ECO:0000313|EMBL:SFR89731.1};
OS Mitsuaria sp. PDC51.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1881035 {ECO:0000313|EMBL:SFR89731.1, ECO:0000313|Proteomes:UP000199246};
RN [1] {ECO:0000313|EMBL:SFR89731.1, ECO:0000313|Proteomes:UP000199246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PDC51 {ECO:0000313|EMBL:SFR89731.1,
RC ECO:0000313|Proteomes:UP000199246};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR EMBL; FOZE01000002; SFR89731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6KER9; -.
DR STRING; 1881035.SAMN05428960_2862; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000199246; Unassembled WGS sequence.
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; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; SSF51905; FAD/NAD(P)-binding domain; 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 Reference proteome {ECO:0000313|Proteomes:UP000199246}.
FT DOMAIN 24..134
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 148..472
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 491 AA; 53245 MW; 3031E17685327BF0 CRC64;
MGKVTGFMEY ERLEEGYEPV EARLKNYKEF VIGLNVEQAK QQGARCMDCG TPFCNSGCPV
NNIIPDFNDL VYRGGDADWK SAIAVLHSTN NFPEFTGRIC PAPCEAACTL NVNDDAVGIK
SIEHAIIDRA WAEGWVPPRP AKVKTGKTVA VVGSGPAGLA AAQQLARAGH SVTVFEKNDR
VGGLLRYGIP DFKMEKSHID RRVQQMEAEG VVFRTGVMVA HLPEGSKVTN WAKDVVTADE
LTEKFDAVLL AGGAEQSRDL PVPGRDLAGV HFAMEFLPQQ NKVNAGDKLK NQLRADGKHV
IVIGGGDTGS DCVGTSNRHG AKSVTQFELM PQPPEVEDRP LTWPYWPIKL RTSSSHEEGC
EREFAIATKE FLGEKGKVTG VKTVRVEWSN GKMVEVPGSE QVLKADLVLL AMGFVSPVAS
IIDAFGVTKD ARGNAKATTD FNGGYKTNAA KVFVAGDMRR GQSLVVWAIR EGRQAARSVD
EFLMGDSALP R
//
