ID A0A0R2A7W8_9LACO Unreviewed; 460 AA.
AC A0A0R2A7W8;
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:KRM61604.1};
GN ORFNames=FC26_GL001680 {ECO:0000313|EMBL:KRM61604.1};
OS Paucilactobacillus vaccinostercus DSM 20634.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1423813 {ECO:0000313|EMBL:KRM61604.1, ECO:0000313|Proteomes:UP000051733};
RN [1] {ECO:0000313|EMBL:KRM61604.1, ECO:0000313|Proteomes:UP000051733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20634 {ECO:0000313|EMBL:KRM61604.1,
RC ECO:0000313|Proteomes:UP000051733};
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:KRM61604.1}.
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DR EMBL; AYYY01000025; KRM61604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2A7W8; -.
DR STRING; 1423813.FC26_GL001680; -.
DR PATRIC; fig|1423813.3.peg.1707; -.
DR Proteomes; UP000051733; 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:UP000051733}.
FT DOMAIN 7..126
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 141..313
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 460 AA; 50566 MW; 7EE7ACCC966043DC CRC64;
MRPVMKRIKD FDVMELDLND EDRRQQAARC MNCGIPFCHH GVFYGDGKAV SGCPNDNLIP
EWNDLVYKNQ DKRAFERLTR TNYLPDMTGR VCPAPCEVSC VNALNGPGVT IRNNEKFIIE
QAFKNGWVVD SGKPAHRTGK KIAVIGSGPA GISAAWRLNQ LGHSVTIFER DDRFGGFLMY
GIPNMKLPKE IVARRFDALR KVGIELVANT EVGKDISAAQ LRQDFDRIVI CTGARQARDL
TVPGRDLDGI YQAADYLKLA TQSVLEDGTA ATTKLAGKHV LVLGGGDTGN DCIGTAIRQG
CAGITQLEIT PALPKERTAE NQWPEWPMVL KNGYGQQEAR SLFGDITRYT ATATGFFGQN
GHVAQVEVSE VSHFQPIDGT QKRIKADLVL LAMGFTGAEQ WLFDEFGVTD KNKDYTTNDG
QLFVAGDCRR GPSLVIWGIH EGRMCAEKVD ASLHALAASR
//
