ID A0A1J5IF82_9GAMM Unreviewed; 1493 AA.
AC A0A1J5IF82;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:OIP95733.1};
GN ORFNames=AUK56_04340 {ECO:0000313|EMBL:OIP95733.1};
OS Thiomicrospira sp. CG2_30_44_34.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Thiomicrospira.
OX NCBI_TaxID=1805397 {ECO:0000313|EMBL:OIP95733.1, ECO:0000313|Proteomes:UP000182935};
RN [1] {ECO:0000313|EMBL:OIP95733.1, ECO:0000313|Proteomes:UP000182935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_44_34 {ECO:0000313|EMBL:OIP95733.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(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}.
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:OIP95733.1}.
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DR EMBL; MNZS01000035; OIP95733.1; -; Genomic_DNA.
DR STRING; 1805397.AUK56_04340; -.
DR Proteomes; UP000182935; 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 20..411
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1493 AA; 163406 MW; BAB67C37FBB22D3F CRC64;
MNSLNSLQGL YSPEFEKENC GFGMIAQMDD KPSHWVVQTA IESLGNMTHR GGVAADGCTG
DGCGLLIKKP DAFLRLEAEK LGIALSQNYA VGMMFLNQDT AKAQTARDTF TDILANKGLS
IAAWRSVPVD SSVLGEQAAG MEPKIEQVFI NAPDALSDGD FNRKLFVARR KTEMQIEPQD
STFYIASLHS QLISYKGLVM PKELPEYYLD LKADHFESSL ISYHQRFSTN TLPQWRLAQP
FRFLAHNGEL NTIKGNRNWA LARQSKFATP LIPDLADLKP LVAQEGSDSN SLDNMLEVLM
MGDMPVFQAL RLLIPPAWQN MPHMDTDLKA FLEYNSMHME PWDGPAGMVI NTGKYAICGV
DRNGLRPTRY MVTKDRHITF ASEIGVYNYA PEDIIEKGRL KPGQVIAVDL ETGTLLKPET
IDATLKSAKP YREWMDKGYM RLEEKLNAQE ALQAWDTTQT DLYQKYFQIT FEERDQIIRV
LAEAGQEATG SMGDDAPLPV FSHKQRSVFD YFRQMFAQVT NPPIDPLREN IVMSLNTCFG
RELNMFDEGE AHARRLETQS PVLSPAMMTQ LTQLNDEYYQ HQRISLHFDT NQTDLKSATI
AVCDQAVAAV KSGITLVILT DQNIEAGKIT VPAAMATGAV HHRLIQEGLR PEANIIVETG
TARDPHHFAV LFGYGATAVF PYLAYESIQD MISTKELDAN TTLAEYIRNY RKGINKGLYK
ILSKMGISTI TSYRGSQLFE AVGLHAEVVD LCFKGTPTRI GGTAFAHLQD DLLKTAQYAF
NPRKYMEAGG LLKYVHGGEY HAYNPDVVNY LREAVQKGDE NAYKKFAQLV NERPAMTLRD
LITFKEGLSP IELNDVEPIE SIFKRFDSAG ISLGALSPEA HEALATAMNR IGARSNSGEG
AEDPARYGTE KMSKIKQIAS GRFGVTAHYL RNAEVIQIKV AQGAKPGEGG QLPGHKVDAT
IAKLRHSVEG VTLISPPPHH DIYSIEDLAQ LIFDLKQVNP NALVSVKLVA EPGVGTIAAG
VAKAYADLIT ISGYDGGTGA SPLTSVKYAG NPFEMGLAET HQVLRANDLR GQVILQADGG
LKTGLDVIKA AILGAESFGF GTAPMIALGC KYLRICHLNT CAVGVATQDE RLRKEHFIGM
PEMVINYFTF VAQETREWLA KLGVAKLEDL VGRVDLLKVI DAPLTDKQRN IDLSGFISDG
GVPKDKPQTV QVERNAPWDK GTLAEAMLAE VLPAIKAKSG GVFEFNLINT GRSIGARIAG
EIAQRYGNNG LKASPITLKL TGIAGQSFGV FNVDGLNLHL HGDANDYVGK GMAGGEIIVC
PAEKAAFDPH TTPIVGNTCL YGATGGKLFA NGTAGERFAV RNSGATAVVE GLGDHGCEYM
TGGCVVSLGS VGVNFGAGMS GGMAFILDTD NTLADRLNSE MVEAIRIDTE STEPYQLYLR
DLLTEYVAKT QSVYGQTVLN QFSRYLNQFW LVKSRAINVD RLLELFASCA DGE
//
