ID A0A0U2YWR5_9BACL Unreviewed; 1527 AA.
AC A0A0U2YWR5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:ALS75998.1};
GN ORFNames=AUC31_12670 {ECO:0000313|EMBL:ALS75998.1};
OS Planococcus rifietoensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=200991 {ECO:0000313|EMBL:ALS75998.1, ECO:0000313|Proteomes:UP000067683};
RN [1] {ECO:0000313|EMBL:ALS75998.1, ECO:0000313|Proteomes:UP000067683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:ALS75998.1,
RC ECO:0000313|Proteomes:UP000067683};
RA See-Too W.S.;
RT "Complete genome of Planococcus rifietoensis type strain M8.";
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013659; ALS75998.1; -; Genomic_DNA.
DR RefSeq; WP_058382701.1; NZ_CP013659.2.
DR STRING; 200991.AUC31_12670; -.
DR KEGG; prt:AUC31_12670; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000067683; 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 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:UP000067683}.
FT DOMAIN 22..420
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 908..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1527 AA; 168378 MW; F2ACF12CC58A4AB3 CRC64;
MSKKEYPIAQ GLYHPDQEHE ACGIGMIANI DGRKSHSIVQ NAVNILCNLE HRGGQSSDTS
TGDGAGILTQ IPHRFFLKQC EKEGIVLPEE GKYGIGMIFM PQDYDLRMKA KDIIQRIVKE
EGQESLGWRP VPVNDSFVGN VAAKTKPVIR QIFIGASAEL ETRMDLERRL YIIRKRIEQE
MGGVEEFKDV YFSSLSAGTI VYKGMLIPEQ LDSFYIDLNH PEFKSALALV HSRFSTNTFP
SWQRSHPNRY SIHNGEFNTL RGNVNWMRAR QLACNSPYFN DQDLQKVLPV IDETGSDSSM
FDNCFEFLHL SGRSLAHTAM MMVPEPWVND KSIDKKKRDF YEYHSTLMEP WDGPAALVFT
DGRQIAACLD RNGLRPARYY ITKSGMIVLG SEVGALDIFS DDIIYKDRLR PGKMLLVDLE
AGKIIPDDEI KTQIASELPY KDWVENNLFD LSDLPEPKEV VHPNSEGLLK QQLAFGYTQE
EVQKIIKPLA SDGKDPVGSM GYDSPLAVLS KKPQLLYNYF KQLFAQVTNP PIDAIREQII
TAARTTIGAE GNLVDPKPES ARHIRLETPV LLNAELERLR QQNLPEFKAV TLPILFEADG
GAEAMEARLE ALFTEADHAI EQGATLVILS DRGVDSTHAA IPALLAVSGL HHHLIRQGTR
TRMSILLESA EPREVHHFAM LIGYGAEGIN PYLAFESIED LVAKDDIHGM NVEQAEASYV
QAVTDGIIKI LSKMGISTIQ SYRGAQIFEA IGIHMDVIDK YFTRTSSRLG GIGLDIIAKE
VLLRHASAYP DREGANPALE SGDEYQYREN GEDHQYNPMT IHTLQQACRT NNYDTFRKYS
KLLTDEKANL QSLRGLLKFK DRTPVPIEEV ETVEEICARF KTGAMSYGSI SKEAHEALAI
AMNKIGGRSN SGEGGEEVSR FIPDDNGDSR RSAIKQVASG RFGVTSHYLV NADEIQIKVA
QGAKPGEGGH LPGKKVYPWI AEVRGSTTGV ELISPPPHHD IYSIEDLAEL IFNLKNANPR
ARISVKLVSA VGVGTIAAGV AKGRADLVLI SGYDGGTGAA PKTSLKHTGL PWEIGLAETH
QTLLLNGLRD RIVVETDGKM MTGRDVVTAA LLGAEEYGFS TAPLVVLGCV MMRVCHLDTC
PVGIATQNPE LRKKYTGEAD HVANFMRFIA MEARELMAEL GFRTINEMIG RTDVLETNKA
IKHWKAEGLD LTQLLYQPDL PEKVGRYATI KQDHGLKHTL DVQELLPRCR NAIENGERVE
VSTAIRNIHR ATGTIIGSAI SRKYGAEGLP EDTITLNFQG SAGQSFGAFI PKGMTLNLIG
DSNDFVGKGL SGGKIIVKPA ADSTFLPEKN IIIGNVSFYG ASAGEAYIHG MAGERFAVRN
SGAKIVVEGV GDHGCEYMTG GRVVILGDTG KNFAAGMSGG VAYVLDEDET FSARCNPEMV
HMQPLADPSE IAELKEMVEN HVRYTGSLNG KRVLDHWEIL SAKFVRVIPK AYLKINERIS
KLQDSGMAKF DAEMAAFEES KMASAGK
//
