ID G5JL42_9STAP Unreviewed; 487 AA.
AC G5JL42;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Glutamate synthase subunit beta {ECO:0000313|EMBL:EHJ07089.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:EHJ07089.1};
GN Name=gltD {ECO:0000313|EMBL:EHJ07089.1};
GN ORFNames=SS7213T_11033 {ECO:0000313|EMBL:EHJ07089.1};
OS Staphylococcus simiae CCM 7213 = CCUG 51256.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=911238 {ECO:0000313|EMBL:EHJ07089.1, ECO:0000313|Proteomes:UP000005413};
RN [1] {ECO:0000313|EMBL:EHJ07089.1, ECO:0000313|Proteomes:UP000005413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 7213 {ECO:0000313|EMBL:EHJ07089.1,
RC ECO:0000313|Proteomes:UP000005413};
RX PubMed=22272658; DOI=10.1186/1471-2164-13-38;
RA Suzuki H., Lefebure T., Pavinski Bitar P., Stanhope M.J.;
RT "Comparative genomic analysis of the genus Staphylococcus including
RT Staphylococcus aureus and its newly described sister species Staphylococcus
RT simiae.";
RL BMC Genomics 13:38-38(2012).
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:EHJ07089.1}.
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DR EMBL; AEUN01000501; EHJ07089.1; -; Genomic_DNA.
DR RefSeq; WP_002464892.1; NZ_AEUN01000501.1.
DR AlphaFoldDB; G5JL42; -.
DR PATRIC; fig|911238.3.peg.1950; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000005413; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EHJ07089.1}.
FT DOMAIN 27..139
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 154..470
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 487 AA; 54795 MW; 17E08481B4CBB42B CRC64;
MGEFKGFMKY NKQYLSELSL VDRLTHHQAY QQRFTKDDAS IQGARCMDCG TPFCQTGQLF
GRETIGCPIG NYIPEWNDLV YRQDFKQAYE RLSETNNFPD FTGRVCPAPC ENACVMKINR
ESVAIKGIER TIIDEAFLNN WVKPKNPKAR RNEKVAIVGS GPAGLTAAEE LNYLGYRVTV
YERAREAGGL LMYGIPNMKL DKEVVRRRIR LMEEAGIIFE TGVEIGVDID KDQLEQQYDA
IILCTGAQKG RDLPLEGRMG AGIHFAMDYL TEQTQLLNGE ITDITITAKD KNVIIIGAGD
TGADCVATAL RENCKSIVQF NKYTKLPEAI TFKENNSWPL AMPVFKMDYA HQEYQAKFGK
EPRAYGVQTM RYDIDNTGHI RGLYTQILQQ SDQGMVMAEG PEKFWPADLV LLSIGFEGTE
TMVPRAFNIK TQHNKIVAND TDYQTNNDKI FAAGDARRGQ SLVVWAIKEG RGVAKAVNQY
LSTKVLV
//
