UniProt: A1VK24

Database: UniProt
Entry: A1VK24_POLNA

LinkDB:  A1VK24_POLNA 
Original site:  A1VK24_POLNA

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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   A1VK24_POLNA            Unreviewed;      1580 AA.
AC   A1VK24;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Glutamate synthase (NADH) large subunit {ECO:0000313|EMBL:ABM36002.1};
DE            EC=1.4.1.14 {ECO:0000313|EMBL:ABM36002.1};
GN   OrderedLocusNames=Pnap_0683 {ECO:0000313|EMBL:ABM36002.1};
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM36002.1, ECO:0000313|Proteomes:UP000000644};
RN   [1] {ECO:0000313|Proteomes:UP000000644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644};
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(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; CP000529; ABM36002.1; -; Genomic_DNA.
DR   RefSeq; WP_011800097.1; NC_008781.1.
DR   STRING; 365044.Pnap_0683; -.
DR   MEROPS; C44.003; -.
DR   KEGG; pna:Pnap_0683; -.
DR   eggNOG; COG0067; Bacteria.
DR   eggNOG; COG0069; Bacteria.
DR   eggNOG; COG0070; Bacteria.
DR   HOGENOM; CLU_000422_8_2_4; -.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000000644; 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:ABM36002.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000644}.
FT   DOMAIN          25..425
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   1580 AA;  173177 MW;  FA044D7717234485 CRC64;
     MTTAAEIKHF EQHGLYAGAN EHDACGVGFV AHIKGHKGHA IVQQALKILE NLDHRGAVGA
     DKLMGDGAGI LIQLPDALYR EEMAAQGVAL PPPGEYGVGM VFLPKEHASR LACEQALERA
     VKAEGQVLLG WRDVPVNRDM PMSPTVREKE PILRQIFIGR GNDVIVQDAL ERKLYVIRKT
     ASAAIQRLKL THSKEYYVPS MSSRTVVYKG LLLADQVGTY FMDLTDVRCV SALGLVHQRF
     STNTFPEWPL AHPYRYVAHN GEINTVKGNY NWMKAREGVM SSPVLGADLQ KLYPISFPGQ
     SDTATFDNCL ELLTMAGYPI SQAVMMMIPE PWEQHTTMDE RRKAFYEYHA AMLEPWDGPA
     SIVFTDGRQI GATLDRNGLR PSRYCVTDDD LVIMASESGV LPIPEHKIVR KWRLQPGKMF
     LIDLEQGRMV DDEEIKATLA HSKPYKQWIE NLRIRLDDVT GKTKESAVTA AAVPGLSLLD
     RQQAFGYTQE DIKFLLSPMA ANGEEATGSM GNDSPLAVLS NKNKQLYNYF KQLFAQVTNP
     PIDPIREAIV MSLVSFIGPK PNLLDINQVN PPMRLEVSQP VLNNADMQKL RDIELRTQGK
     FKSYTLDITY PLAWGREGVE AKLASLCAEA VDAIKGGNNI LIVSDRALSA TQVAIPALLA
     LSAIHQHLVK EGLRTTAGLV VETGSAKEVH HFAVLAGYGA EAVHPYLALE TLAELSKGLP
     GDLSTEKAVY NYTKAIGKGL SKIMSKMGVS TYMSYCGAQL FEAIGLNRQT VDKFFTGTSS
     QVEGMGVFEI AEEALRMHKA AFSDDPVLSN MLDAGGEYAW RVRGEDHMWT PDTIAKLQHS
     TRANNWNTYK EFAQLVNDQN RRHMTLRGLF EFKIDPSKAI PIDEVEPAKE IVKRFVTGAM
     SLGSISTEAH ATLAVAMNRI GGKSNTGEGG EDPARYRQEL KGIPIKRGDT LKSVIGEKVV
     EVDLPLQDGD SLRSRIKQVA SGRFGVTAEY LVSADQIQIK MAQGAKPGEG GQLPGGKVSE
     YIGQLRFSVP GVGLISPPPH HDIYSIEDLA QLIHDLKNVN PRASISVKLV SETGVGTIAA
     GVAKAKADHV VIAGHDGGTG ASPWSSIKHA GSPWEIGLAE TQQTLVLNRL RGRIRVQADG
     QMKTGRDVVI GALLGADEFG FATAPLVVEG CIMMRKCHLN TCPVGVATQD PVLRRKFSGK
     PEHVVNYFFF VAEEARQLMA QLGVRKFDDL IGRPDLLDMQ KGVEHWKASG LDFSRLFYQP
     QVPADVPRLH VMDQDHGLDR ALDMRLIEKS RAALEKGEKV QFIEVARNVN RTVGAMLSGE
     LTRLRPEGLP DDTLRIQLEG TGGQSFGAFL AKGITLYLIG DANDYTGKGL SGGRIVVRPS
     IDFRGDAVKN TIVGNTVMYG ATSGESFFSG VAGERFAVRL SGATTVVEGT GDHGCEYMTG
     GTVAVLGKTG RNFAAGMSGG VAYVYDEDGQ FATRCNTSMV SMDRVVTTAE QHTHDKSDWH
     AGESDEEQLK RLLQDHNRWT GSKRARELLD TWSVSRLKFV KVFPNEYKRA LIERQERRLE
     AATETTSAQV ATNQEAVLAK
//

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