ID A0A150F9C8_9BACI Unreviewed; 1520 AA.
AC A0A150F9C8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:KXZ21762.1};
GN ORFNames=AXI58_12525 {ECO:0000313|EMBL:KXZ21762.1};
OS Bacillus nakamurai.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1793963 {ECO:0000313|EMBL:KXZ21762.1, ECO:0000313|Proteomes:UP000075430};
RN [1] {ECO:0000313|EMBL:KXZ21762.1, ECO:0000313|Proteomes:UP000075430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-41092 {ECO:0000313|EMBL:KXZ21762.1,
RC ECO:0000313|Proteomes:UP000075430};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|ARBA:ARBA00001927};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
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:KXZ21762.1}.
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DR EMBL; LSBA01000006; KXZ21762.1; -; Genomic_DNA.
DR RefSeq; WP_061521127.1; NZ_LSBA01000006.1.
DR STRING; 1793963.AXI58_12525; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000075430; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 2.160.20.60; Glutamate synthase, alpha subunit, C-terminal domain; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR002489; Glu_synth_asu_C.
DR InterPro; IPR036485; Glu_synth_asu_C_sf.
DR InterPro; IPR006982; Glu_synth_centr_N.
DR InterPro; IPR002932; Glu_synthdom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR11938; FAD NADPH DEHYDROGENASE/OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11938:SF133; GLUTAMATE SYNTHASE (NADH); 1.
DR Pfam; PF00310; GATase_2; 1.
DR Pfam; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR Pfam; PF01493; GXGXG; 1.
DR SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 22..415
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 890..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1520 AA; 167967 MW; 0B73BBFBDBAA47B9 CRC64;
MTYNQMPKAQ GLYRPEFEHD ACGIGLYAHL KGEPSHDIVK KGLKMLCQLD HRGGQGSDPN
TGDGAGLMVQ IPDAFLKKEC GEMKLPEKGR YGVGMVFFSQ NEEERKKIEK QVNTLIEQEG
QTVLGWRTVP VNVGKIGTVA QNTCPYVRQI FIGASVDLKD SLAFERKLYV IRKQAENWGA
AEQLDFYFAS LSSQTIVYKG LLTPEQVDAF YLDLQDEAFV SAFSLVHSRF STNTFPTWER
AHPNRYLIHN GEINTLRGNI NWMKAREQQF VSESFGDDLQ KVLPILNADG SDSSILDNAF
EFFVMAGRKP AHTAMMLIPE PWTENTHMSK AKRAFYEYHS SLMEPWDGPT AISFTDGKQI
GAILDRNGLR PARYYVTKDD HIIFSSEVGV IETEQENILQ KKRLEPGKML LIDLEEGRII
SDEEVKTEIA NEFPYQKWLE EELVQVNPDP EIREEEQFAD LLVRQKAFGY TYEDIQKYLI
PVIKEGKDPL GSMGNDAPLA VLSDRAQSLF NYFKQLFAQV TNPPIDAIRE QLVTSTVTWL
GAEGDLLHPS ERNARRIKLY TPVLSNEQFY ALKTIVHPDV KSENIHMLFS DDLEKGLQDL
FDQAEKAINQ GVSLLILSDK AMTEELTPIP PLLAVSALHQ HLIRQGLRTK ASIIVESGEA
REVHHFAALI GYGADAVNPY LTYATFKQEI DEGRLDINYE EAVSKYGKSI TEGVVKVMSK
MGISTVQSYR GAQIFEAVGI SRDVIGQYFT GTASQLGGIG LETIAEEAKQ RHQAAYKDDY
SKTLDSGSEF QWRNGGEHHA FNPKTIHTLQ WACRKNDYSL FKQYSHAADE ERIGFLRNLF
AFQEDRKPLR VEEVESAASI VKRFKTGAMS FGSLSKEAHE ALAIAMNRLG GKSNSGEGGE
DPKRFVPDEN GDDRRSAIKQ IASARFGVKS HYLVNADELQ IKMAQGAKPG EGGQLPGNKV
YPWVADVRGS TPGVGLISPP PHHDIYSIED LAQLIHDLKN ANRDARISVK LVSKAGVGTI
AAGVAKGTAD VIVVSGYDGG TGASPKTSIK HTGLPWELGL AEAHQTLMLN GLRERVVLET
DGKLMTGRDV VMAALLGAEE FGFATAPLVV LGCVMMRACH LDTCPVGVAT QNPELRKKFM
GDPDHIVNYM LFVAEEVREY MAQLGFKTFD EMIGRTDVLH VSERAKAHWK ASQLDLSTLL
YQPEGVRTFR TAQNHKIDQS LDMTDILPSV KEAIEAGKEA EVEIKINNTN RVAGTVTGSE
ISKRYGAEGL PDDTIKLHFT GSAGQSFGAF VPKGMTLHLN GDSNDYVGKG LSGGKIIVKA
PDAFTCETQD NVIIGNVAFY GATSGEAYIN GCAGERFAVR NSGVNVVVEG IGDHGCEYMT
GGRVVVLGEV GKNFGAGMSG GIAYVLADDA KAFKRKCNLE MISFEKLTDE TEIQEVKAMV
EKHAALTNSQ KAASLLDNWE ETVQTFIKII PTNYKQMLLS IEEQKAAGLS EEDAIMYAFE
ANTKQAKQAP SQGQKQAVVQ
//
