ID I0JT47_HALH3 Unreviewed; 495 AA.
AC I0JT47;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Glutamate synthase small subunit {ECO:0000313|EMBL:CCG47319.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:CCG47319.1};
GN Name=gltB1 {ECO:0000313|EMBL:CCG47319.1};
GN OrderedLocusNames=HBHAL_4982 {ECO:0000313|EMBL:CCG47319.1};
OS Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS 3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG47319.1, ECO:0000313|Proteomes:UP000007397};
RN [1] {ECO:0000313|EMBL:CCG47319.1, ECO:0000313|Proteomes:UP000007397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA Oesterhelt D.;
RT "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT salinities by the moderately halophilic, chloride-dependent bacterium
RT Halobacillus halophilus.";
RL Environ. Microbiol. 15:1619-1633(2013).
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR EMBL; HE717023; CCG47319.1; -; Genomic_DNA.
DR RefSeq; WP_014645203.1; NC_017668.1.
DR AlphaFoldDB; I0JT47; -.
DR STRING; 866895.HBHAL_4982; -.
DR KEGG; hhd:HBHAL_4982; -.
DR PATRIC; fig|866895.3.peg.4021; -.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_000422_3_1_9; -.
DR Proteomes; UP000007397; Chromosome.
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 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; SSF51905; FAD/NAD(P)-binding domain; 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 ECO:0000313|EMBL:CCG47319.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007397}.
FT DOMAIN 24..139
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 154..477
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 55025 MW; 0A3F2C8DF612F6ED CRC64;
MGKSTGFMEY ERQSIPERDP ATRTKDWEDY TLPMSDEEAQ KQGARCMDCG VPTCHSGMEV
KGMTTGCPVY HLIPEWNDLV YRGQWKEALK KEHEMNNFPE FTGFACPAPC EGACVLGINE
PPVAIRSVER SIIEKGFAEG WVVPEPPEKR TGRSVAVVGS GPAGLAAAAQ LNKAGHWVTV
FERSDRVGGL LTYGIPEMKL PYEIVERRVN ILKEEGIRFQ TNTEVGRDYP VSRLNEEYDS
VILCGGATTP RNLEVDGRGL KGIHYAMDFL YANTKSLLDS NHEDKNYISA KDKNVIVIGG
GDTGTDCIST SVRHECKTLT QFDIYDKKGS ERDNEVNPWP QYPIIHTVGY GQKEAEAKFG
DDPRAYAVMT KKFVGDENNR IKEVHTIDVA LSFDDEGNKV RTEIPGTEKV WPADLVLLAI
GFSGPEQDLI EKLGIETTVR TNVAAQYGKY TTNVEGVFAA GDMRRGQSLI VWAINEGREV
ARECDRFMMG STQLP
//
