ID   A0A1H0MXM5_9PSEU        Unreviewed;      1520 AA.
AC   A0A1H0MXM5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Glutamate synthase (NADPH/NADH) large chain {ECO:0000313|EMBL:SDO85219.1};
GN   ORFNames=SAMN05192558_105105 {ECO:0000313|EMBL:SDO85219.1};
OS   Actinokineospora alba.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=504798 {ECO:0000313|EMBL:SDO85219.1, ECO:0000313|Proteomes:UP000199651};
RN   [1] {ECO:0000313|Proteomes:UP000199651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M 10655 {ECO:0000313|Proteomes:UP000199651};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FNJB01000005; SDO85219.1; -; Genomic_DNA.
DR   STRING; 504798.SAMN05421871_102155; -.
DR   Proteomes; UP000199651; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199651}.
FT   DOMAIN          31..426
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   1520 AA;  165061 MW;  A8BA8F439A109320 CRC64;
     MKTVEGRRSM IFSALPSPMG LYDPAAERDA CGVAMVADIH GRRSHAIVTD ALTALANLEH
     RGAAGAEPTS GDGAGILVQL PDELLRAEAG FELPEPDELG RNRYATGLAF LPADADDRAK
     AVELVERIAE EEGLRVLGWR DVPVDPVGAG LGPTALSVMP HFAMPFLEAA ESDLAGIELD
     RHVYCLRKRV EHAGSEIYFP SLSSRTLVYK GMLTTAQVPA FFADLRDERL TSAIALVHSR
     FSTNTFPSWP LAHPFRYVAH NGEINTVRGN RNRMRAREAL LASDRIPGDL TRLYPIVDPN
     GSDSASFDEV LELLHLGGRS LPHAVLMMIP EAWENHATMD PKRRAFYRFH NSLMEPWDGP
     ACVTFTDGTL VGAVLDRNGL RPARWWRTKD DRIVLASETG VLDVPPSEVV AKGRLKPGRM
     FLVDTEAGLI VDDDQVKSEL ADQLPYEEWL HAGLLKIADL ADREHVVQTH ESVQRRQVTF
     GYTEEEVKIL LTPMAITGAE PIGSMGTDTP PAALSQRSRL LYDYFKQNFA QVTNPPLDAI
     REEIVTSVRR IMGPEQNLLE PGPASCRHIQ LPYPVIDNDE LAKLIHVNDD GDLPGYASTV
     LSGLYEVDGG GAALASAIER VRREASAAIE AGARILVLSD RDSDHRMAPI PSLLLVSAVH
     HHLVRTKERL RVALVVESGD AREVHHIALL LGYGAAAVNP YLAFETIEDL ITHGAITGVE
     PRTAIRRYVQ ALVKGVLKIM SKMGISTVGA YTAAQVFESF GLAQDVLDEY FTGTLSKLGG
     VGLDVIARES QSRHRRAHPE NPTDRVYRRL EVGGEYAYRR EGELHLFTPE TVFLLQHATK
     TGREDVYREY SAEVDRLNRE GGALRGMFAM KTEGRTPIPI DEVEPVESIL RRFNTGAMSY
     GSISAEAHET LAIAMNSIGG RSNTGEGGED PDRLHDPRRR SAIKQVASGR FGVTSEYLVH
     ADDIQIKMAQ GAKPGEGGQL PPNKVYPWIA RTRHSTAGVG LISPPPHHDI YSIEDLAQLI
     HDLKNANENA RVHVKLVSEA GVGTVAAGVS KAHADVVLIS GHDGGTGASP LNSLKHAGTP
     WEIGLAETQQ TLMLNGLRDR ITVQVDGALK NGRDVIVAAL LGAEEFGFAT APLVVAGCVM
     MRVCHLDTCP VGVATQNPVL RKRYTGQAEH VVNYFRFVAQ EVREHLAALG FRTIDDAVGH
     AELLDVDKAV SHWKTEGMNL APVFEVAPVS GARRRVRAQD HGLAEALDRT MMRLAEPALE
     DALPVRLELP VRNVNRTVGT LLGAEVTRRY GDTLPEDTVH VTLTGSAGQS LGAFLPKGIT
     LDLVGDANDY VGKGLSGGRI IVRPHPEAPF AAERQVIAGN VIAYGATSGE VFLRGCVGER
     FGVRNSGAVI VAEGVGDHAF EYMTGGRAVV LGKTGRNLAA GMSGGIGYVL ALDPAKVNPA
     MVEIQRPGFD DLRWLREIVA KHHKATGSAV AASLLGDWTR RAAAFAKVMP RDYQRVLEAM
     RIARVEGRDV DEAVMEASRG
//