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Database: UniProt
Entry: A0A077M2K2_9MICO
LinkDB: A0A077M2K2_9MICO
Original site: A0A077M2K2_9MICO 
ID   A0A077M2K2_9MICO        Unreviewed;       486 AA.
AC   A0A077M2K2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Glutamate synthase (Small subunit) {ECO:0000313|EMBL:CCH79237.1};
DE            EC=1.4.1.13 {ECO:0000313|EMBL:CCH79237.1};
GN   Name=gltB {ECO:0000313|EMBL:CCH79237.1};
GN   ORFNames=BN12_4080006 {ECO:0000313|EMBL:CCH79237.1};
OS   Tetrasphaera japonica T1-X7.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Tetrasphaera.
OX   NCBI_TaxID=1194083 {ECO:0000313|EMBL:CCH79237.1, ECO:0000313|Proteomes:UP000035721};
RN   [1] {ECO:0000313|EMBL:CCH79237.1, ECO:0000313|Proteomes:UP000035721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T1-X7 {ECO:0000313|EMBL:CCH79237.1,
RC   ECO:0000313|Proteomes:UP000035721};
RX   PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA   Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA   Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA   Nielsen K.L., Nielsen P.H.;
RT   "A metabolic model for members of the genus Tetrasphaera involved in
RT   enhanced biological phosphorus removal.";
RL   ISME J. 7:543-554(2013).
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCH79237.1}.
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DR   EMBL; CAJB01000344; CCH79237.1; -; Genomic_DNA.
DR   RefSeq; WP_048555759.1; NZ_HF570958.1.
DR   AlphaFoldDB; A0A077M2K2; -.
DR   STRING; 1194083.BN12_4080006; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000035721; Unassembled WGS sequence.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
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   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; 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   ECO:0000313|EMBL:CCH79237.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035721}.
FT   DOMAIN          27..128
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          146..455
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   486 AA;  52173 MW;  1D4D5DAF241E4CB5 CRC64;
     MADPQGFLKV RERELPTRRP VPVRILDWHE VYEPQPVEEL QRQAGRCMDC GIPFCHTGCP
     LGNLIPEWND LAWKGDWHEA IERLHATNNF PEFTGRLCPA PCETACVLGI NQPAVTIKQV
     EVTTIERAFA AGDVAPQPPD RLSGKTVAVV GSGPAGLAAA QQLTRAGHTV AVYERADKPG
     GLLRYGIPEF KMEKAIVDRR IAQMEAEGTR FRSGVDVGVD VTGDQLLSRY DAIVLAVGST
     VPRDLPVPGR ELDGVLQAMD FLPPANRAAL GETVEGQVTA EGKDVIVIGG GDTGADCIGT
     AHRQGARSVT SLEIMPQPPQ DRPTSQPWPT YPMIYRVASA HEEGGERVYA VSTSEIVGDE
     QGRVAGLRLH EVVMGESGFE KVEGTERELP AQLILLAMGF LGPQGEGVVD QLGVERDARS
     TIVRDRSFMT SVPGVFVAGD AGRGQSLIVW AIAEGRSAAA GVDAYLTGAP SQLPRPIEPT
     TRPLVV
//
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