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Database: UniProt
Entry: K6W5Y5_9MICO
LinkDB: K6W5Y5_9MICO
Original site: K6W5Y5_9MICO 
ID   K6W5Y5_9MICO            Unreviewed;       485 AA.
AC   K6W5Y5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Glutamate synthase small subunit {ECO:0000313|EMBL:GAB77237.1};
GN   Name=gltD {ECO:0000313|EMBL:GAB77237.1};
GN   ORFNames=AUCHE_05_01420 {ECO:0000313|EMBL:GAB77237.1};
OS   Austwickia chelonae NBRC 105200.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC   Austwickia.
OX   NCBI_TaxID=1184607 {ECO:0000313|EMBL:GAB77237.1, ECO:0000313|Proteomes:UP000008495};
RN   [1] {ECO:0000313|EMBL:GAB77237.1, ECO:0000313|Proteomes:UP000008495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 105200 {ECO:0000313|EMBL:GAB77237.1,
RC   ECO:0000313|Proteomes:UP000008495};
RA   Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Ohji S.,
RA   Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Austwickia chelonae NBRC 105200.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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:GAB77237.1}.
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DR   EMBL; BAGZ01000005; GAB77237.1; -; Genomic_DNA.
DR   RefSeq; WP_006501989.1; NZ_BAGZ01000005.1.
DR   AlphaFoldDB; K6W5Y5; -.
DR   STRING; 100225.SAMN05421595_1053; -.
DR   eggNOG; COG0493; Bacteria.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000008495; 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; IPR017896; 4Fe4S_Fe-S-bd.
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.
DR   PROSITE; PS51379; 4FE4S_FER_2; 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:UP000008495}.
FT   DOMAIN          37..69
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   485 AA;  52868 MW;  96BAC788D8A891E0 CRC64;
     MADPQGFLTH RERKLPPRRP VPVRLTDWRE VNESQDVEEL RDQASRCMDC GIPFCHSGCP
     LGNIIPEWND LAWRGRWGEG IERLHATNNF PEFTGRLCPA PCESSCVLGI NQQAVTIKQV
     EVTTIERAFD DGRVTPLPPE RLSGRTVAIV GSGPAGLSAA QQLTRAGHTV AVFERADKAG
     GLLRYGIPEF KMEKSVLDRR LAQMRAEGTR FRTGVDIGVE ITGQELRRRY DAIVLATGST
     IPRDLDIPGR NGRGVVQAMD YLPQANRSAL GQPIEDQIVA TDKDVIVIGG GDTGADCIGT
     ALRQGARSVT SLEIMPQPPT ARNEAHPWPT YPVLFRVASA HEEGGERLYA VNTKEFVNDE
     NGELCALKLS EVRLEDGRFQ EIEGTERELP TQLVLLAMGF TGTERDGVVA QLGVGVDGRG
     QVVRDQNYMS TVPGVFAAGD CGRGQSLIVW AIAEGRACAH GVDEWLTGSS VLPRPVGPRD
     RPLTV
//
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