ID A0A0M2LLZ4_9MICO Unreviewed; 1543 AA.
AC A0A0M2LLZ4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KKI16883.1};
GN ORFNames=XM48_13500 {ECO:0000313|EMBL:KKI16883.1};
OS Leucobacter sp. Ag1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI16883.1, ECO:0000313|Proteomes:UP000033836};
RN [1] {ECO:0000313|EMBL:KKI16883.1, ECO:0000313|Proteomes:UP000033836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI16883.1,
RC ECO:0000313|Proteomes:UP000033836};
RA Pei D., Kukutla P., Yu W., Xu J.;
RT "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) 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 -!- 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:KKI16883.1}.
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DR EMBL; LAYO01000107; KKI16883.1; -; Genomic_DNA.
DR RefSeq; WP_046456408.1; NZ_LAYO01000107.1.
DR STRING; 1642040.XM48_13500; -.
DR PATRIC; fig|1642040.3.peg.2493; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000033836; 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; 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:UP000033836}.
FT DOMAIN 32..435
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1543 AA; 166206 MW; 2E6C624BD596F195 CRC64;
MRTTPATPNP AVTSGFPAAT GLYRPEDERD ACGLAAIVAL TGAPGHEVIS QALEALEHLE
HRGAVGSDAG TGDGAGILSD LPDALIRAEL AEHDPEAVLP EPGRYAAGLA FLPQSSTERR
AVRYRIAAIA AEESLDVIAW RPVSVRSEVL GESAREAAPR IEQLILAPRV DEAGGAALLG
QVRPIDTDEL ERRAFRTRKR VQNETGVYLP SLSARTIVYK GMVTTLQLSG FYPELSDERF
ASRFAIVHSR YSTNTFPSWH LAQPLRLVAH NGEINTVRGN RNWMRAREAQ LESDRLGDVR
QLAPICSDGG SDSASFDEVL ELLVMAGRSL PHALAMMVPE AWESERGLSP ELVEFLEYHS
LLMEPWDGPA AMIATDGTEL VALLDRNGLR PGRYLVTSDG TMVIASETGV LDIAPERVVK
RGRLQPGRML AVNLATGEIR DDETVKNELA GLAPWGEWLD EGRIRLSDQP EREHLMHPPA
SITRRQRTFG YTDEELRLLL TPMAREGIEP IAAMGTDTPI AVLSERPRLI FDYFVQQFAQ
VTNPPLDALR EELITSLRAG MGPQENLLTQ SAAHARQVIL DFPVIDNDAL ARIQHFGEDF
ERERAVALRG LYPVDFGAKG LADRLEALCW EASAAVDAGA EFLVISDRDS NKDLAPVPSL
LAVSAVHHHL IREGQRMRVA LIAEAGDVRE VHHVAALIGY GAAAVNPYLA METVGLLVRD
GSIGGVTEEQ AIARLIKGLG KGMLKVMSKM GISTVASYCG AQTFEAVGLA QDVVDRYFTG
TASRLGGVGL DVIAAEVAAR HRSAYPDDAA TLAHQRLATG GEYRWRRGEE PHLFDPETIY
KLQHATRTGR REIFSEYTRR VNEQQERLMT LRGLFRFSAQ RPPVPLGEVE PVSEIVKRFA
TGAMSYGSIS PEAHQTLAIA MNRLGGKSNT GEGGESDERL IDPERRSAIK QVASGRFGVT
SMYLTNADEI QIKLAQGAKP GEGGQLPPAK MYPWIARTRH ATPGVGLISP PPHHDIYSIE
DLKQLIFDLK RANPSARIST KLVAQSGIGP VAAGVAKALS DVILVSGHDG GTGASPMNSL
KHAGSPWELG LAEAQQTLML NGLRERVVLQ ADGQLKTGRD VVIAALLGAE EFGFATAPLV
VSGCIMMRVC HLDTCPVGVA TQNPELRERF TGQAEHVVNF FRFIAEEVRE ILASLGYRTL
DEAVGDTAAL DVDDAIRHWK ADGLDLSPIL RGPDFDESAP RRSGREQDHE LAEHFDAGLI
EISTDALERR EPVIIDLPIS NIDRAVGTML GHEVTRRFGA EGLAPATIDV TLTGSAGQSL
GAFLPTGIAL RLVGDANDYV GKGLSGGEIS IRPDPNAGHP AADNVIAGNV IGYGATSGSL
WIAGVVGERF MVRGSGATAV VEGTGDHALE YFTGGFALIL GPTGRNIGAG MSGGEAVLLD
LDPADVNAAE LGSGDLLLTP VPQELRERIV GLLGRHVEQT GSELAETLLG DIETDPEAAF
ARFTRIIPKN YSRVLEIRER AGATGADPDG EQVWNEILEA THG
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