UniProt: Q3JAR7

Database: UniProt
Entry: Q3JAR7_NITOC

LinkDB:  Q3JAR7_NITOC 
Original site:  Q3JAR7_NITOC

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (7)   
   Pfam (4)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (22)   

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ID   Q3JAR7_NITOC            Unreviewed;      1554 AA.
AC   Q3JAR7;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Glutamate synthase (NADH) large subunit {ECO:0000313|EMBL:ABA58079.1};
DE            EC=1.4.1.14 {ECO:0000313|EMBL:ABA58079.1};
GN   OrderedLocusNames=Noc_1604 {ECO:0000313|EMBL:ABA58079.1};
OS   Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS   11848 / C-107).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Nitrosococcus.
OX   NCBI_TaxID=323261 {ECO:0000313|EMBL:ABA58079.1, ECO:0000313|Proteomes:UP000006838};
RN   [1] {ECO:0000313|Proteomes:UP000006838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19707 / BCRC 17464 / NCIMB 11848 / C-107
RC   {ECO:0000313|Proteomes:UP000006838};
RX   PubMed=16957257; DOI=10.1128/AEM.00463-06;
RA   Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA   Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA   Vergez L.M., Ward B.B.;
RT   "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT   oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL   Appl. Environ. Microbiol. 72:6299-6315(2006).
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; CP000127; ABA58079.1; -; Genomic_DNA.
DR   RefSeq; WP_011330708.1; NC_007484.1.
DR   STRING; 323261.Noc_1604; -.
DR   MEROPS; C44.003; -.
DR   KEGG; noc:Noc_1604; -.
DR   eggNOG; COG0067; Bacteria.
DR   eggNOG; COG0069; Bacteria.
DR   eggNOG; COG0070; Bacteria.
DR   HOGENOM; CLU_000422_8_2_6; -.
DR   InParanoid; Q3JAR7; -.
DR   Proteomes; UP000006838; Chromosome.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016040; F:glutamate synthase (NADH) 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:ABA58079.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006838}.
FT   DOMAIN          22..421
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   1554 AA;  170741 MW;  9636980C881168A9 CRC64;
     MSDGTLPRKQ GLYDPHNEHD SCGVGFVANV KGHKSHNLIR KGLQILKNLT HRGAVGADPR
     AGDGAGILLQ MPDQFLQEEC ARQGINLPPV GEYGVGMLFL PQGAEARATC EELISHYIDA
     EGQTLLGWRD VPTDNTQLGE SVKAVEPIIR QVFIGHGDNT SSGDPFERKL FVIRKQIENA
     VRELDQADQA TFSIPSLSSR ILVYKGMLLA SQVPSYFTDL TDERMITALS LVHQRFSTNT
     FPSWDLAQPF RMIAHNGEIN TLRGNINWMA ARRHAMTSKL LGDDLKKLWP LIAEGQSDSA
     CFDNALELLV AGGYPLAHAM MLLIPEAWAG NPLMEAKQRA FYEYHAALME PWDGPAAMAF
     TDGRMIGATL DRNGLRPARY LITNDDLVAM ASEMGVLDIP QERIIKKWRL QPGKMLLIDL
     EAGRIIDDDE LKRKLAEAEP YQQWLDQTQI RIEHLPAETG PMAPDPATLL DRQQAFGYTQ
     EDLKFLLTPM AVTGQEAVGS MGADEPLAVL SNRAIPLSNY FKQRFAQVTN PPIDPIREEL
     VMSLVSLIGP RPNLLGHHHQ AGAHKRLEVS QPVLTNTDLE RIRRIEDHTG GAFRTHTLTI
     CYPVTEGAAG MEAALGKLCR SAEQAVHKGY NILILSDRGV DIDHVAIPAL LATSAVHHHL
     VQTGLRTETG LVVETGAARE VHHFAVLAGY GAEAINPYLA FETLSALRQQ LPEELNEEEI
     QKRYIKAVGK GLLKIMSKMG ISTYQSYCGA QIFDGVGLSH NFVEKYFTGT VSTIEGAGLS
     EIAEEAFRWH RNAYSDVPLY RHGLDAGGYY AYRLRGEDHM WTFDTISKLQ HASRANEAKT
     YEEYAQLVNQ QNKRLLTLRG LLEFRFAANP LPLEDVEPAK DIVKRFATGA MSFGAISHEA
     HTTLAIAMNR IGGKSNTGEG GEEAERFKPL PNGDSMRSAI KQVASGRFGV TAEYLVNADD
     IQIKMAQGAK PGEGGQLPGH KVDATIAQVR HSTPGVGLIS PPPHHDIYSI EDLAQLIFDL
     KNVNPQARIS VKLVSEVGVG TVAAGVSKAH ADHVTIAGHD GGTGASPLTS IKHAGLPWEI
     GLAETQQTLV LNRLRGRIAV QVDGGIRTGR DVVIGALLGA DEFGFATAPL IVAGCIMMRK
     CHLNTCPTGV ATQDPVLRKL FTGKPEHIVN YFFLVAEEVR QIMAQLGFRC FDEMIGRLDV
     LDTRQALDHW KAKGLDFSRI LYHPTTDPEV PLYNRERQDH GLDEVLDRWL IAQAQPALER
     QEAVQIETPV GNTDRTVGAM LSGEVARRYG HKGLPQDTIY IRTEGTAGQS FGAFLAHGIS
     LELIGEANDY VGKGLSGGRL VITPPPECPI VPEENIIIGN TVLYGAISGE CYFRGVAGER
     FAVRNSGVTA VVEGVGDHGC EYMTGGVVVV LGRTGRNFAA GMSGGIAYVL DEAGNFEQRC
     NLAMVELEPI AEEDEALEHL EHQGGDLETH GRVDISHHIS RFDGQRLRNL IEKHQHYTHS
     GRARQILENW SAYLPRFVKV MPVDYRRALQ EMEHAQAARH TIPVMQQEAL DQYG
//

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