ID A0A0R1VKF7_9LACO Unreviewed; 474 AA.
AC A0A0R1VKF7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Glutamate synthase subunit beta {ECO:0000313|EMBL:KRM05765.1};
GN ORFNames=FC89_GL001474 {ECO:0000313|EMBL:KRM05765.1};
OS Liquorilactobacillus ghanensis DSM 18630.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423750 {ECO:0000313|EMBL:KRM05765.1, ECO:0000313|Proteomes:UP000051451};
RN [1] {ECO:0000313|EMBL:KRM05765.1, ECO:0000313|Proteomes:UP000051451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18630 {ECO:0000313|EMBL:KRM05765.1,
RC ECO:0000313|Proteomes:UP000051451};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM05765.1}.
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DR EMBL; AZGB01000018; KRM05765.1; -; Genomic_DNA.
DR RefSeq; WP_057872197.1; NZ_AZGB01000018.1.
DR AlphaFoldDB; A0A0R1VKF7; -.
DR STRING; 1423750.FC89_GL001474; -.
DR PATRIC; fig|1423750.3.peg.1512; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000051451; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000051451}.
FT DOMAIN 23..138
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 157..458
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 474 AA; 52075 MW; 07D8152455489948 CRC64;
MADPFGFMKY PRETNPYRDV KERIKDFAEM QLPLSDEERR KQAARCMNCG VPHCHAGFFY
AGGKAVSGCP NDNLIPEWND LVYRQEDKRA FERLTKTNPL PEFTGRVCPA PCEVACNEAL
NGQGITIKDN ERFIIEQGFK FDWVIDSGMP QHRNGIKIAV IGSGPAGLSA AWQLNKFGFD
VTVYERDDRP GGLTMYGIPN MKLPKEIVSR RIAAMEAVGI KFIVNTEVGV DITAAELKAQ
YQRIILTVGA RSARDLAVPG RELKGVMQAV DFLTQATKEV LQNGTKATKL LAGKKVVVIG
GGDTGNDCIA TAVRQGAAEI HQLEITRQPP KQRLASNPWP QWPMVAKTGY GQQEAQTLFG
DKLTAYETTA VGFSGKDGRV TQMTTSKARL FKPVAGTEQD QPVDLVLLAM GFTGPQKSVM
DAFGITQIND DYSTNEESVF VAGDARRGPS LVIWGIHEGR MVADQVAHSC EVRL
//