ID A0A077M9U4_9MICO Unreviewed; 1513 AA.
AC A0A077M9U4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutamate synthase (Large subunit) {ECO:0000313|EMBL:CCI52615.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:CCI52615.1};
GN Name=gltA {ECO:0000313|EMBL:CCI52615.1};
GN ORFNames=BN13_190020 {ECO:0000313|EMBL:CCI52615.1};
OS Tetrasphaera jenkinsii Ben 74.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1193518 {ECO:0000313|EMBL:CCI52615.1, ECO:0000313|Proteomes:UP000035720};
RN [1] {ECO:0000313|EMBL:CCI52615.1, ECO:0000313|Proteomes:UP000035720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ben 74 {ECO:0000313|EMBL:CCI52615.1,
RC ECO:0000313|Proteomes:UP000035720};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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:CCI52615.1}.
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DR EMBL; CAJC01000101; CCI52615.1; -; Genomic_DNA.
DR RefSeq; WP_048544955.1; NZ_HF571038.1.
DR STRING; 1193518.BN13_190020; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000035720; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:CCI52615.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035720}.
FT DOMAIN 25..412
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1513 AA; 163168 MW; 1EC52D1B0AE94CE6 CRC64;
MTRLPFSALP PDSGLYRGAN EHDACGVAMV ATLRGTAGHD IVRHALTALT NLDHRGATGA
DPLVGDGAGI LTQVPDAFLR GVVPFTLPAR GSYAVGMVFL PIDLDERARA MARIEDLAVE
EGLEVFGWRD VPHLPELVGA AARDCMPHFA QLFVGASNGA MRGIHLDRRA YCLRKRAERE
LDIYVASLSA RTVVYKGMLT TGQLEPFFPD LSDERFATEL ALVHSRFSTN TFPSWPLSHP
YRLIAHNGEI NTVKGNRNWM AARESQLQSD LIPGDLERLF PICPPGQSDS ASFDEVLELL
HLGGRSLPHA VLMMIPEAWE NHEEMDPDRR AFYEFHSLTM EPWDGPACIT FTDGTLIGAV
LDRNGLRPGR YWITEDGLVV LASEAGVLDL APETVVRKGR LQPGRMFLVD TAQGRIIEDE
EVKSALATQL PYADWLHAGL IELGELPERE HIVHTAKSVA RRQQTFGYTQ EELRIILAPM
ARTGIEALGS MGTDSPIAVL SSKPRLLFDY FTQQFAQVTN PPLDAIREEL VTSLGVAVGP
EGNLLTATPA HARQLVLPFP VIDNDELAKI IRINADGDLP GYATAVIKGL YDVHGGAEAL
QARLAEIFAE VSAAIAGGAR FVVLSDRDSN RDLAPIPSLL LCSAVHHHLI REKTRTQVGL
VIETGDVREV HHVALLIGYG AAAVNPYLAM ESVEDLVRSG ALTGVTGEKA VKNLIKALGK
GVLKVMSKMG ISTVASYRGA QVFEAIGLSQ ELVDAYFTGT VSQLGGVGLE VIAAECAARH
AAAYPTDGVR LPHRRLEVGG EYQWRREGEP HLFDPETVFR LQHSTRQRRY DIFKQYTARI
DDQAQRLMTL RGLFAFKEGL RPPVPIEEVE PVTEIVKRFN TGAMSYGSIS LEAHQTLAIA
MNRLGGRSNT GEGGEDLDRL LDPERRSAIK QVASGRFGVT SAYLTHANDI QIKMAQGAKP
GEGGQLPGHK VYPWVAKTRH STPGVGLISP PPHHDIYSIE DLAQLIHDLK NANPEARIHV
KLVAEVGVGT VAAGVSKAHS DVVLISGHDG GTGASPLTSL KHAGGPWELG LAETQQTLVL
NGLRDRIVVQ VDGQLKTGRD VVIAALLGAE EFGFATAPLV VSGCIMMRVC HLDTCPVGVA
TQNPELRARF TGKPEFVETF FEYIAEEVRE HLAALGFRSI AEAIGEVATI DTSAAVDHWK
ANGLDLAPLL QEAIPAEGTT RYQSISQDHG LEKALDHQLI ALARPALDDG EQARGTLAIR
NVNRTVGTLL GHEVTRRHVG GLPDGSIDLT LTGSAGQSFG AFLPAGVTLR LVGDANDYVG
KGLSGGRLIV TPAPESTFVA ADNVIAGNVI GYGATTGEIF LRGTAGERFC VRNSGATAVV
EGVGDHACEY MTGGTVLILG RIGRNFAAGM SGGYAYVLDL PEHRVNRELV DILPVAGAHA
EVVESLLRRH HEHTGSALAA ALLADLPSAL ERFRLVLPRD YQRVLDVRAA AESEGLDLDG
DVVWDRIMEA SRG
//
