ID   Q0PCB8_CAMJE            Unreviewed;      1496 AA.
AC   Q0PCB8;
DT   19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   19-SEP-2006, sequence version 1.
DT   02-SEP-2026, entry version 100.
DE   RecName: Full=Glutamate synthase [NADPH] large chain {ECO:0000256|ARBA:ARBA00072108};
DE            EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
DE   AltName: Full=Glutamate synthase subunit alpha {ECO:0000256|ARBA:ARBA00079921};
GN   Name=gltB {ECO:0000313|EMBL:CAL34188.1};
GN   OrderedLocusNames=Cj0007 {ECO:0000313|EMBL:CAL34188.1};
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 /
OS   NCTC 11168).
OC   Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC   Campylobacterales; Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222 {ECO:0000313|EMBL:CAL34188.1, ECO:0000313|Proteomes:UP000000799};
RN   [1] {ECO:0000313|EMBL:CAL34188.1, ECO:0000313|Proteomes:UP000000799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000313|Proteomes:UP000000799};
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K., Ketley J.M., Churcher C., Basham D.,
RA   Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K.,
RA   Karlyshev A., Moule S., Pallen M.J., Penn C.W., Quail M., Rajandream M.A.,
RA   Rutherford K.M., VanVliet A., Whitehead S., Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 L-glutamate + NADP(+) = L-glutamine + 2-oxoglutarate + NADPH
CC         + H(+); Xref=Rhea:RHEA:15501, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58359; EC=1.4.1.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00048151};
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; L-glutamate biosynthesis via GLT
CC       pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+)
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00037898}.
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; AL111168; CAL34188.1; -; Genomic_DNA.
DR   PIR; B81416; B81416.
DR   RefSeq; WP_002853155.1; NC_002163.1.
DR   RefSeq; YP_002343479.1; NC_002163.1.
DR   AlphaFoldDB; Q0PCB8; -.
DR   SMR; Q0PCB8; -.
DR   STRING; 192222.Cj0007; -.
DR   PaxDb; 192222-Cj0007; -.
DR   EnsemblBacteria; CAL34188; CAL34188; Cj0007.
DR   GeneID; 904339; -.
DR   KEGG; cje:Cj0007; -.
DR   PATRIC; fig|192222.6.peg.7; -.
DR   eggNOG; COG0067; Bacteria.
DR   eggNOG; COG0069; Bacteria.
DR   eggNOG; COG0070; Bacteria.
DR   HOGENOM; CLU_000422_8_2_7; -.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019676; P:ammonia assimilation cycle; IEA:TreeGrafter.
DR   CDD; cd00982; gltB_C; 1.
DR   CDD; cd00713; GltS; 1.
DR   CDD; cd02808; GltS_FMN; 1.
DR   FunFam; 2.160.20.60:FF:000001; Glutamate synthase, large subunit; 1.
DR   FunFam; 3.60.20.10:FF:000001; Glutamate synthase, large subunit; 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; IPR050711; ET-N_metabolism_enzyme.
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   NCBIfam; NF008730; PRK11750.1; 1.
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   FAD {ECO:0000256|ARBA:ARBA00022827};
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   ECO:0000256|PROSITE-ProRule:PRU00609};
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:CAL34188.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000799}.
FT   DOMAIN          25..416
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   ACT_SITE        25
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00609"
SQ   SEQUENCE   1496 AA;  166720 MW;  0244E98A5099ABCD CRC64;
     MDLENILENN QSIGLYHPKN EHDACGIAAV ANIRGIASYK VICDALEILM NLEHRGGTGA
     EENSGDGAGI LIQIPHDFFK TQELGFELPK KGDYAVAQMF LSPNTDAKEE AKEIFLQGLK
     DKKLEFLGFR EVPFNPSDIG ASALKAMPYF LQAFVKKPSK ISAGLEFERV LYSTRRLIEK
     RAINVPKFYF SSFSSRTIVY KGMLLSTQLS DFYLDFKDVN MKSAIALVHS RFSTNTFPSW
     ERAHPNRYMV HNGEINTIRG NVDSIRAREG LMQSEYFENL DEIFPIIAKL SSDSAMFDNT
     LEFLALNGRT LEEAFMMMVP EPWHKNENME SKKRAFYEYH SLLMEPWDGP AAIVFTDGVI
     MGASLDRNGF RPSRYYLTKD DMLILSSETG ALKLDEKNIK AKKRLEPGKL LLVDTARGRV
     IADNEIKEHY ANAKPYKKWL KNLVELEKQK SGVYKHQFLK EDEVLKLQKA FGWSYDELKM
     SVAAMAQNGK EAIAAMGVDT PLAILSKTYQ PLYNYFKQLF AQVTNPPLDA IREEIVTSTR
     IYLGSEGNLL KPDENNAKRV KIALPVISNE ELFEVKALNK FQVKEFSILY DYSKKTLEKA
     LDELCVKIED EVKKGVSIII LSDKGVDEKN AYIPALLAVS GVHNHLVRKN LRTHTSLIIE
     SGEPREIHHF ACLLGYGATV INPYLVYESI QKLIANKDLN LSYEKAVENF IKASSSGIVK
     IASKMGVSTL QSYNGSALFE CLGLSSKVID KYFTSTTSRI EGMDLEDFEK ELIALHKHAF
     NDTHKALDSK GIHGFRSAKE EHLIDPLVIF NLQQACRNKD YKSFKKYSAL VDEKQVNLRS
     LMEFDFSEAI SIDKVESVES IVKRFRTGAM SYGSISKEAH ECLAQAMNKI GAKSNSGEGG
     EDEERYEIKE GVDKNSAIKQ VASGRFGVDL NYLSHAKEIQ IKVAQGAKPG EGGQLMGFKV
     YPWIAKARHS TAGVTLISPP PHHDIYSIED LAQLIYDLKH ANKDAKISVK LVSENGIGTV
     AAGVAKAGAN LILVSGYDGG TGASPRTSIP HAGIPWELGL AETHQTLILN KLRDRVRLET
     DGKLMNGRDL AIAALLGAEE FGFATAPLIV LGCTMMRVCH LNTCPFGIAT QDTELRDRFK
     GKVDDVINFM YFIAEELREY MARLGFERLD DMIGRVDKLR QKSVQGKAGK LNLDKILKSL
     PTYNRTAVHF KDYKDNKLEK TIDYRILLPL CKNAVEKKEP IKLSLEVGNQ SRTFATMLSS
     EILKTYGKDA LDEDSIHIKA IGNAGNSFGA FLLKGIKLEI IGDSNDYLGK GLSGGKIIAK
     ISNEATFSPE ENIIAGNACL YGATKGEVYL DGIAGERFCV RNSGALAVVL GTGVHGCEYM
     TGGQVVVLGD VGANFAAGMS GGVVYIFGRH NEAHVNTELV DIKDLNAKDE KELKAVIEKH
     ITYTDSKKAK DILEKFDKKD FFKVMPRDYE KMLKMLDLCK NEKDPNLAAF LKITQK
//