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}.
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; 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
//