ID C7MVF6_SACVD Unreviewed; 1527 AA.
AC C7MVF6;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Glutamate synthase (NADH) large subunit {ECO:0000313|EMBL:ACU97785.1};
GN OrderedLocusNames=Svir_28040 {ECO:0000313|EMBL:ACU97785.1};
OS Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / NBRC
OS 12207 / P101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=471857 {ECO:0000313|EMBL:ACU97785.1, ECO:0000313|Proteomes:UP000000841};
RN [1] {ECO:0000313|EMBL:ACU97785.1, ECO:0000313|Proteomes:UP000000841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101
RC {ECO:0000313|Proteomes:UP000000841};
RX PubMed=21304650; DOI=10.4056/sigs.20263;
RA Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Chain P., D'haeseleer P., Chen A., Palaniappan K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Rohde M., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Saccharomonospora viridis type strain
RT (P101).";
RL Stand. Genomic Sci. 1:141-149(2009).
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; CP001683; ACU97785.1; -; Genomic_DNA.
DR STRING; 471857.Svir_28040; -.
DR MEROPS; C44.003; -.
DR KEGG; svi:Svir_28040; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_11; -.
DR Proteomes; UP000000841; Chromosome.
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:UP000000841}.
FT DOMAIN 29..432
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1527 AA; 165346 MW; 303CDDA0D0F78932 CRC64;
MTTQGVPLIF SAIPEKQGVY DPAAEKDACG VAMIAHVKGV RSHGIVTDGL TALMNLDHRG
AAGAEPTSGD GAGILVQLPD DFLRAEVDFA LPEPDERGRH RYAAGLVFLP AEAEARARAV
RTVERIATEE NLVVLGWREV PTAPDAAEVG PTARSVMPHF AMLFVAEAPN ADGDRRAGVD
LDRLAFCLRK RAEHETLAAE CGVYFPSLSA RTLVYKGMLT PTQLPVFFPD LRDERLTSAI
ALVHSRFSTN TFPSWPLAHP FRFVAHNGEI NTIRGNRNRM RAREALLDSD LIPGDLSRLF
PVCSPDGSDS ASFDEVLELL HLGGRSLPHA VLMMIPEAWE NHRTMDPARR AFYQFHASLM
EPWDGPACVT FTDGSLVGAV LDRNGLRPAR WWRTADDRVV FASESGVLDV PAGEVVAKGR
LKPGRMFCVD TEAGRVVDDD EIKADLAAQA PYEEWLRAGL LSLDKLPERQ HVPQSHASVL
RRQLTFGYTE EELKVLLAPM ALKGAEPVGS MGSDTPPSVL SKRSRLLYEY FKQGFAQVTN
PPLDAIREEL VTSLSRVMGP EQNLLAPGPA SCRQIQLDSP VIDNDELAKL IHVNADGDLP
GFSCTVLSGL YEVDGGGEAL AEAIERVRKE ASQAVEAGAH ILVLSDRGSD HRMAPIPSLL
LVSAVHHHLV RTKERLRVAL VVETGDAREV HHIALLLGYG AAAVNPYLAF ESIEDLIAQG
AVSGVDAPTA VRNYITALNK GVLKIMSKMG ISTVGAYTGA QVFEALGLSQ DVLDEYFTGT
VSPLGGVGLD VLAEEVAIRH RRAYPENPAE RAHRGLESGG DYAYRREGEL HLFTPETVFL
LQHASASRRW EVYRRYVDEV NRLNREGGVL RGMFAFREGV RKPVPIEEVE SVESICRRFN
TGGMSYGSLS LEAHQTLAVA MNTIGGRSNS GEGGEEPDRL HDPLRRSAVK QVASGRFGVT
SEYLVSADDI QIKMAQGAKP GEGGQLPPHK VYPWIAKTRH STPGVGLISP PPHHDIYSIE
DLAQLIHDLK NANERARIHV KLVSSLGVGT VAAGVAKAHA DVVLISGHDG GTGASPMNSL
KHAGTPWEIG LAQTQQTLML NGLRDRITVQ VDGGFKTGRD VVVAALLGAE EYGFATAPLV
VAGCVMMRVC HLDTCPVGVA TQNPALRERF TGRAEHIVNF FRFVAQEVRE YLARLGFRSL
DEVIGRADLL DVDEAVEHWK AKGLDLSPIF AVPSRGGARR KVREQDHGLD RALDRTLVQL
AEAALEDARP VRLELPVRNV NRTVGTLLGS EVTRRYGSTG LPDDTIHVRL TGSAGQSLGA
FLPPGVTIDL VGDANDYVGK GLSGGRIIVR PDPEAPFAAE DQVIAGNTLA YGATSGELFL
RGQVGERFGV RNSGALLVAE GVGDHAFEYM TGGYAVVLGG TGRNVAAGMS GGIAYVLRLD
ERDVNPEMVE LHTPDEEDLA WLRDVVERHH RLTGSPVAAS LLGDWKRRSA AFVKVMPTDY
RRVLEAMEAA KAQGRDVDEA IMEAARG
//
