ID A0A0F7FS31_9ACTN Unreviewed; 487 AA.
AC A0A0F7FS31;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Glutamate synthase subunit beta {ECO:0000313|EMBL:AKG42338.1};
GN ORFNames=SXIM_09540 {ECO:0000313|EMBL:AKG42338.1};
OS Streptomyces xiamenensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=408015 {ECO:0000313|EMBL:AKG42338.1, ECO:0000313|Proteomes:UP000034034};
RN [1] {ECO:0000313|Proteomes:UP000034034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A01550 {ECO:0000313|Proteomes:UP000034034};
RA Xu J.;
RT "Complete genome sequence of a mangrove-derived Streptomyces xiamenensis.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR EMBL; CP009922; AKG42338.1; -; Genomic_DNA.
DR RefSeq; WP_030734139.1; NZ_CP009922.3.
DR AlphaFoldDB; A0A0F7FS31; -.
DR STRING; 408015.SXIM_09540; -.
DR KEGG; sxi:SXIM_09540; -.
DR PATRIC; fig|408015.6.peg.983; -.
DR HOGENOM; CLU_000422_3_1_11; -.
DR Proteomes; UP000034034; 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; 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}.
FT DOMAIN 38..69
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 52651 MW; FF29033A23DFE2EA CRC64;
MADPKGFLTT GRETATSRPA AERVKDWNEV YVPGSLLPII SKQASRCMDC GIPFCHNGCP
LGNLIPEWND YAYREDWAAA SERLHATNNF PEFTGRLCPA PCESACVLGI NQPAVTIKNV
EVTIIDKAWE AGNVTPQPPQ RHSGKTVAVI GSGPAGLAAA QQLTRAGHTV AVYERADRIG
GLLRYGIPEF KMEKRHINRR IEQMRAEGTK FRTGVEIGRD IDAAKLRKRY DAVVIAAGAT
TARDLPVPGR ELNGVHQAME YLPLSNKVQE GDFITAPISA EGKHVVVIGG GDTGADCVGT
AHRQGAASVT QLEIMPRPSE DRPAHQPWPT FPMTYKVTSA HEEGGERVYS VSTTHFEGDE
DGNVQWLHLV EVEFIDGKLT QKPGTERKIP AQLVTLAMGF TGTDQENGLV RQFGVDLDAR
GNIARDADYA TSVDGVFVAG DAGRGQSLIV WAIAEGRAAA RGVDRFLTGA PSALPYPIRP
TDRSLTV
//
