UniProt: Q8CWY9

Database: UniProt
Entry: Q8CWY9_STRMU

LinkDB:  Q8CWY9_STRMU 
Original site:  Q8CWY9_STRMU

All links

Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (7)   
   Pfam (4)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (23)   

Download RDF

ID   Q8CWY9_STRMU            Unreviewed;      1505 AA.
AC   Q8CWY9;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   SubName: Full=Glutamate synthase (Large subunit) {ECO:0000313|EMBL:AAN58123.1};
DE            EC=1.4.1.13 {ECO:0000313|EMBL:AAN58123.1};
GN   Name=gltA {ECO:0000313|EMBL:AAN58123.1};
GN   OrderedLocusNames=SMU_365 {ECO:0000313|EMBL:AAN58123.1};
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN58123.1, ECO:0000313|Proteomes:UP000002512};
RN   [1] {ECO:0000313|EMBL:AAN58123.1, ECO:0000313|Proteomes:UP000002512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA   Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN58123.1; -; Genomic_DNA.
DR   RefSeq; NP_720817.1; NC_004350.2.
DR   RefSeq; WP_002279635.1; NC_004350.2.
DR   SMR; Q8CWY9; -.
DR   STRING; 210007.SMU_365; -.
DR   MEROPS; C44.003; -.
DR   KEGG; smu:SMU_365; -.
DR   PATRIC; fig|210007.7.peg.319; -.
DR   eggNOG; COG0067; Bacteria.
DR   eggNOG; COG0069; Bacteria.
DR   eggNOG; COG0070; Bacteria.
DR   HOGENOM; CLU_000422_8_2_9; -.
DR   OrthoDB; 9758182at2; -.
DR   PhylomeDB; Q8CWY9; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
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   ECO:0000313|EMBL:AAN58123.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002512}.
FT   DOMAIN          23..401
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   1505 AA;  166629 MW;  1E5B4FDA3ECCD5B1 CRC64;
     MREVIKKAKQ TTLWDPSFET DACGMGFVAQ IDGIASHQLV DYALTMLERM NHRGGTGAEP
     DTGDGAGMLL AMPDEFFRLK AKEEEIDLPP LGDYAVAQLF LPQDKVAKTI LEDSLISEIK
     RLGFHVLLSR DVPFNYDNCG PAAQEIMPSF VQLFIEKPTE TNSGCAFEDS LFRLRRKLEK
     TFAADELFIC SLSSKTIVYK GMLHAFQVRL FYPDLSDEMF KSHIALTHSR FSTNTFPSWD
     RAQPFRFLAH NGEINTLRGA ENWMHSHQIE VYNEENSDSA KLENCLEYLY RHGRDIPQSL
     LMMVPEAWGK DAGLSKELTA FYEYASSFVA PWDGPAALVF TDGEMVGARL DRNGLRPSRY
     SRTKDNFLIC SSESGVVDIA PSQVVEKGVL GPGNMMLIDT KKNLVLKNDE VKEHYSKQHP
     YQQWVQENVT LLDDFAAQEE IVNDYDVNQM WKIFGYTDET IRTVILPMSE KGEEPVISMG
     FDSPLAVLSK KPQSLFTYFK QQFAQVTNPP IDAIREQLVV STTVFLGGDG DIRQDNADNC
     VKVRVDSPVL SSQDFAKLAN LTDERYKATT LSTVYDLGDS DNNRLQYALE DLFKKADEAI
     NQGSKIIILS DRGVTKGRIA IPILLAVSGL NNYMVVKGKA SQFSIVVDTA EAFEVHHFAT
     LVGFGATAIH PYGAYATLKA FDKTNDSFEK YRKAAEKGIV KVMSRMGIST VLGYKGAQLF
     EAIGLSADVV NQYFRGTATR IEGLSLKQIE KEYLERVDFA FGPRANDFLP SGGSYQYKTD
     GEYHLFNPRS IYNFQQSIRR GDYGLFKQYS TELDNEALKQ PTTLRSLWEF HSKRPKVDLA
     EVEPAKEIVK RFKVGAMSFG SLSKEAHETI AQAMNTIGAK SNSGEGGENR KRFKPQVDGR
     NINSKIKQVA SGRFGVNAEY LMSAEELQIK LAQGAKPGEG GQLPGQKVFP WIAEIRGATP
     GVRLISPPPH HDIYSIEDLA QLIYDLKAIN PYAKINVKLV SSTGVGTIAT GCVKAGADKV
     VISGYDGGTG ASPRNSVRDA GLPWEMGLAE AHQTLSMNRL RQRMTLETDG KLMTGRDIAI
     ATLLGAEEYS FASLALISVG CVMMRVCSLN TCPVGVATQN PELRKNFSGK PEHVINMMTF
     LAEELREYMA ELGFRSVDEM VGHAEVLKSR FVAQGKAKSL NFSRVIGNSF PIDRKNEDPF
     AEERQWKELD GFAAAAIEKG ISVTIENTIN NVDRSVGSRM AGWMAERYGN DAVKEGLIKY
     HYTGIAGQSF ASYLTQGLEY TLIGEANDYI AKSMSGGRLI VKPPHDAAYD VENSPIVGNV
     SLFGAVKGEA YFAGRAGERF CVRNSGAKVV VEGVGAHGCE YMTGGVAVIL GTTGRNFAAG
     MSGGVAYVYD VHGDFAQKVN MEMVDLYQIG ETRGDDILKD MIEKHYEYTE SVKAKRLLDN
     WDEEVKRFIK VYPSDFHEIN DIEYALSQKG MSGDELELRT FEVATGGDAT AQERQALLAS
     VTGGK
//

DBGET integrated database retrieval system