ID A0A1L3MR15_9BACI Unreviewed; 1522 AA.
AC A0A1L3MR15;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:APH04783.1};
GN ORFNames=A9C19_08505 {ECO:0000313|EMBL:APH04783.1};
OS Bacillus weihaiensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1547283 {ECO:0000313|EMBL:APH04783.1, ECO:0000313|Proteomes:UP000181936};
RN [1] {ECO:0000313|EMBL:APH04783.1, ECO:0000313|Proteomes:UP000181936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alg07 {ECO:0000313|EMBL:APH04783.1,
RC ECO:0000313|Proteomes:UP000181936};
RX PubMed=27901120; DOI=10.1038/srep38248;
RA Zhu Y., Chen P., Bao Y., Men Y., Zeng Y., Yang J., Sun J., Sun Y.;
RT "Complete genome sequence and transcriptomic analysis of a novel marine
RT strain Bacillus weihaiensis reveals the mechanism of brown algae
RT degradation.";
RL Sci. Rep. 6:38248-38248(2016).
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}.
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DR EMBL; CP016020; APH04783.1; -; Genomic_DNA.
DR RefSeq; WP_072579576.1; NZ_CP016020.1.
DR STRING; 1547283.A9C19_08505; -.
DR KEGG; bwh:A9C19_08505; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000181936; Chromosome.
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 Coiled coil {ECO:0000256|SAM:Coils};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000181936}.
FT DOMAIN 22..415
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 890..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 436..463
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1522 AA; 167891 MW; 93E3D0BDCF0BD9CA CRC64;
MTYNQIPKAQ GLYRPEFEHD ACGIGLYAHI KGHATHDIVK KGLSMLCQLD HRGGQGSDPL
TGDGAGLMVQ IPDAFFKKTC TEMSLPANGR YGVGMMFFSN DDAERHQIEE QLNKFIEAEG
QILLGWRDVP VNAEEIGPVA KLSCPVVRQV FIGAKDNQID QLTFERKLYI IRKQAENWAR
EKELRFYFTS LSSSTIVYKG LLTPEQVDAF YLDLQDEDFV SAFSLVHSRF STNTFPSWER
AHPNRYLIHN GEINTLRGNM NWMKAREQQF VSEAFGDDLK KILPILDADG SDSSILDNAF
EFFVLAGRKP AHAAMMMIPE PWTENPHMSP EKRAFYEYHS CLMEPWDGPT AISFTNGKQI
GAILDRNGLR PARYYVTKDD YIIFSSEVGV IEVEESDVLY KDRLSPGKML LIDLEEGRII
SDKEIKDEMA NEKPYQEWLK EQLVKLEDQS ELLQEEVVSD INERQVAFGY TYEDIQKYLL
PVITEGKDPL GSMGNDTPLA VLSERPQSLF NYFKQLFAQV TNPPIDAIRE QIVTSSMTLL
GTEGNILHPS KENAKRIQLD SPVLTNDQLA QLRLNLHPGF QATTLHTLFT EDLDYSIKNL
CAEADKAIED GVNILILSDR MMNKENAAIP ALLAVGALHQ HLVRQGTRTK ASLVIESGEA
REVHHFAALI GYGVDAINPY LAFATYKEAV ADGSLDFEYQ EVIEKYCKAV TEGVIKVMSK
MGISTVQSYR GAQIFEAVGI SAEVVDRFFT GTASQLGGID LDTIAQEALI RHQGAYAEKI
DKALDSGSDF QWRKNGEHHA FNPTTIHTLQ WACRKNDYGL FKKYSDAANE ERIGFLRNLF
SFKSSRASIS IDEVESVESI VKRFKTGAMS FGSLSKEAHE TLAIAMNRLG GKSNSGEGGE
DPNRFAPDAN GDLRRSAVKQ IASGRFGVKS HYLVNADELQ IKMAQGAKPG EGGQLPGNKV
YPWVADVRGS TPGVGLISPP PHHDIYSIED LAQLIHDLKN SNRDARISVK LVAKAGVGTI
AAGVAKGAAD VIVISGYDGG TGASPKTSIK HTGLPWELGL AEAHQTLMLN GLRDRVVLET
DGKLMTGRDV AMAAILGAEE YGFATAPLVV MGCIMMRVCH LDTCPVGVAT QNPDLRDKFT
GDPDHIVNYM RFVAQEVREI MAELGFRTME EMVGSTDVLE VSDRAKAHWK AKHLDLSTLL
YQPEGARTAT LKQNHKIEQS LDMVEILPAV KEAIESATPI DASFSIKNIN RVTGTIVGSE
ISKRYGEEGL PEDTVTLRFN GSAGQSFGAF VPKGVTMHLT GDANDYLGKG LSGGKIIVKP
SLDSNIVASD NVIIGNVPFY GATSGEAYIN GRAGERFAVR NSGVNVVVEG VGDHGCEYMT
GGKVVILGEV GKNFGAGMSG GIAYVLADDS EEFKTICNDE MIEFEQLASV DEILFLKEMI
QNHIDYTGSA KGRFVLDNWN ETLTKFVKVI PKDYKRMMNR ISEQMEAGLS NEEAIMSAFE
ANAKSEKKGP MNKTNRSKAV LQ
//