ID A0A0X8D461_9BACL Unreviewed; 1497 AA.
AC A0A0X8D461;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:AMA74066.1};
GN ORFNames=ACH33_15400 {ECO:0000313|EMBL:AMA74066.1};
OS Aneurinibacillus sp. XH2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=1450761 {ECO:0000313|EMBL:AMA74066.1, ECO:0000313|Proteomes:UP000065566};
RN [1] {ECO:0000313|Proteomes:UP000065566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xh2 {ECO:0000313|Proteomes:UP000065566};
RA Xi L.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMA74066.1, ECO:0000313|Proteomes:UP000065566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xh2 {ECO:0000313|EMBL:AMA74066.1,
RC ECO:0000313|Proteomes:UP000065566};
RA Zhang Z., Qiao N., Zhang Y., Xiao Z., Jing L., Zhao J.-Y.;
RT "Draft genome of the novel themophilic polyhydroxyalkanoates producer
RT Aneurinibacillus sp. XH2 (CCTCC M 2013550) isolated from Gudao oilfield in
RT China.";
RL Submitted (JAN-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}.
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DR EMBL; CP014140; AMA74066.1; -; Genomic_DNA.
DR RefSeq; WP_057899793.1; NZ_CP014140.1.
DR STRING; 1450761.ACH33_15400; -.
DR KEGG; anx:ACH33_15400; -.
DR Proteomes; UP000065566; 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; cd02808; GltS_FMN; 1.
DR CDD; cd00504; GXGXG; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000065566}.
FT DOMAIN 20..390
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1497 AA; 163169 MW; 4FD19609A0E8337F CRC64;
MKRADFGNFR NHLAEEHDSC GIIAIIEKNG KPNRDNISKI IDGLIKMEHR SGFIDGEGDG
CGILSDIPRD LWAKKLADAG KPAELAYSPS FAVGHIFIPT KGHNVHSVME NIRSMFTKAN
LVIELEQINN VNSEVLGKNG RADEPVFWQL ACKYTGNYVI EKELFELLIA IEKKHNVHVA
SLSNHSASYK VMGAANILPQ YFQDIQQPEF ASSVTVGHNR YSTNTLSNFF RVQPFTIIGH
NGEINTIRKL EDEGEMLGVD LVEGGSDSQN MNRAIETLIH RYDLSLFEAM EMVFPPIINE
MKSLRPELQD LYVYYRQTWG HYAQGPAGIV SRYANECVFS VDALGLRPLW MVESEASLYF
SSEQGVIPVY EMVSEPKALA PGEKVGVQLN PGQPITVVPH HELQNIVLER SSKRMDFTGF
RNQLSFSQVK AAKTPYEDIE TVTNQQYAAY GWEREHIQLA EQMASSGAEP IRSLGHDAPL
AAIAEARQNI TDFIKESVAV VTNPAIDRER EMEHFSTRIV LGGRPGLFPQ EGKATAALEL
PSPLLFEGKA LQELAGKLNT VSLEQLLEHF GTDAHVLPVY FTREESIPQA LERIAKSAVD
AVKNGARILL FDDSMAHRDG RYWIDPHLVI SKADRALKEA GAKGNGNLRR QASIIMRSGA
LRNLHDLAVA FGLGADAVAP YLLFTTVFLK DREHSVENLY HALNKGLEKV ISTIGIHELR
GYARLFSSIG LNSEVAEVLG IVNFCGSDKA GTSFAELEAD SKARYEDWNN EQAKPAKIFH
MWPRIWKSIG EVASGSLPYT EFANKLLEQE RENPLSIRHL ADFDTSKANK EVSPEQVDIS
IGDHSLPFLI SSMSFGSQNE VAFRAYAEAA EQLNMISLNG EGGEIKDMLG KYRKTRGMQV
ASGRFGVNVE LANSSNLLEI KIGQGAKPGE GGHLPGKKVT AKVAAARNAT LGSDLISPSN
NHDIYSIEDL AQIITELKTA NSEAKVCVKV PVVPNIGTIS VGIAKAGADY ITLSGFDGGT
GAARVHALQH VGLPVEIGVK AAHTALIEAG LRDKVELWAD GGIKSGHDVV KMILLGANRI
GFGTLAMLAV GCTTCRGCHL DTCHVGIATQ IESVEEAKEH GLRRFVPRIF DVAVDNLKRL
FTALGEEVKR ITAELGFERL QDMVGRADLL VQTRGLNKMD LSALLTSAPF PLLKSERVES
KVLVAVGAET YEASDQYASP YAPINETFTN VLSDQRVLGS RYSGARVKPY LDGSYVNLPE
VSLTFDRGSV PGNGLAAFNA EGVFIRVHGG AQDGVGKTGF GGRVAIMKSP NANRQFINGS
VGKSFCYGAQ KGLYIVQGNA DARACIRLSG ADVVIGGELQ EPINDRLGGI GARANIKGFA
FEYMTNGRAI VLGDPGPWIC SGMTGGVVYL RVQPEMGLDQ AALERRIAKA AKVSLKPLDA
KGKEDVAYLL GEYITELKAS GQQDKAASIQ NLIDNAEQHF IMVSPVKEQA DPSIATE
//
