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Database: UniProt
Entry: A0A1G5NPL3_AFIMA
LinkDB: A0A1G5NPL3_AFIMA
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ID   A0A1G5NPL3_AFIMA        Unreviewed;       479 AA.
AC   A0A1G5NPL3;
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:SCZ39327.1};
GN   ORFNames=SAMN03080610_02433 {ECO:0000313|EMBL:SCZ39327.1};
OS   Afifella marina DSM 2698.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Afifellaceae; Afifella.
OX   NCBI_TaxID=1120955 {ECO:0000313|EMBL:SCZ39327.1, ECO:0000313|Proteomes:UP000199347};
RN   [1] {ECO:0000313|EMBL:SCZ39327.1, ECO:0000313|Proteomes:UP000199347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2698 {ECO:0000313|EMBL:SCZ39327.1,
RC   ECO:0000313|Proteomes:UP000199347};
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; FMVW01000005; SCZ39327.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5NPL3; -.
DR   STRING; 1120955.SAMN03080610_02433; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000199347; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199347}.
FT   DOMAIN          24..133
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          147..460
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   479 AA;  53224 MW;  1626A45957A93C2E CRC64;
     MAKVTGFLEI DRQEQRYQPA SDRIRHFKEF VLPLPEPEVR RQASRCMDCG IPYCHGPTGC
     PVHNQIPDWN DLVWQDDWEE AARNLHSTNN FPEWTGRICP APCEEACTLN LEDAPVTIKT
     VEQAVADKAF QEGWIRPQPA ERKTGKRIAI IGSGPAGMAA AQQLARVGHD VHVYEREPKA
     GGLCRYGIPD FKMEKYHIDR RVTQMEGEGV IFHYGVNIGV TTPMKELVDE HDAVLIATGS
     ERPRDPGIGG MELTGVHYAM PYLIQSNRRV NGEPVPEIDH PDDIWAGRRH VVVVGGGDTA
     SDCVGTAFRQ GAISVTQLDI RACPPEKENK ALVWPYWPTK LRTSSSQAEG AEREFQAATL
     EFVGKNGVLT GVKCARVDEK RQPLEGTEFI LKADLAFIAI GFAGPLEDTF VKEFGGALKQ
     DRRTNILADE KSYRTSVDKV FAAGDVRRGQ SLVVWAIREG RQAARSIDQF LMGETSLPL
//
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