ID A0A0U1QL83_9BACL Unreviewed; 486 AA.
AC A0A0U1QL83;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KLI01559.1};
GN ORFNames=SINU_12840 {ECO:0000313|EMBL:KLI01559.1};
OS Sporolactobacillus inulinus CASD.
OC Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Sporolactobacillus.
OX NCBI_TaxID=1069536 {ECO:0000313|EMBL:KLI01559.1, ECO:0000313|Proteomes:UP000035553};
RN [1] {ECO:0000313|EMBL:KLI01559.1, ECO:0000313|Proteomes:UP000035553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CASD {ECO:0000313|EMBL:KLI01559.1,
RC ECO:0000313|Proteomes:UP000035553};
RX PubMed=21952540; DOI=10.1128/JB.05934-11;
RA Yu B., Su F., Wang L., Xu K., Zhao B., Xu P.;
RT "Draft genome sequence of Sporolactobacillus inulinus strain CASD, an
RT efficient D-lactic acid-producing bacterium with high-concentration lactate
RT tolerance capability.";
RL J. Bacteriol. 193:5864-5865(2011).
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:KLI01559.1}.
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DR EMBL; AFVQ02000188; KLI01559.1; -; Genomic_DNA.
DR RefSeq; WP_010024904.1; NZ_AFVQ02000188.1.
DR AlphaFoldDB; A0A0U1QL83; -.
DR STRING; 1069536.SINU_12840; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000035553; 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; 2.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 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:UP000035553}.
FT DOMAIN 24..140
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 153..317
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 395..467
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 486 AA; 53392 MW; FEA2F15D352F63B3 CRC64;
MGQLMGFMNI EKKNQSERKP VERVRDWNEY KIPLTEKEVK KQAARCMDCG TPYCQIGTVI
NRGTTGCPLH NLIPEWNDLV YHGLWKEAYE RLAKTNNFPE FTSRACPAPC EGSCTAGLVS
DSVSIKSIER AIIDRAFEEG WITPKPPKRR TGKKVAVIGS GPAGLACADQ LNKIGHEVTV
FERSDRPGGL LMYGIPSMKI EKDVVDRRVQ LLKDEGIHFE TNADVGKTIS VASLKEAYSA
VILCTGAGKH REVSLEGRAL KGISPAMDYL TASNRNQLYG EPLADDFDAK GKNVIVIGGG
DTGEDCVATA IRQGCKSVVQ FGKHGKLPAK RAENNPWPEH PNVFSVDYAY KDAEEVFGND
PREYYVETKK FVGDDNGHVK ELLTGSFKKE ANGAAAHKTW NADLVLIAIG FQGAEDQVFD
AFDVKRDSSG RVIEADTIRY QTSKDGIFAA GDARRGASLI VWAIEEGRRA AAAVDLYLDK
KLSVLN
//
