ID Q4KJI6_PSEF5 Unreviewed; 1482 AA.
AC Q4KJI6;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 2.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Glutamate synthase, large subunit {ECO:0000313|EMBL:AAY95862.2};
DE EC=1.4.1.13 {ECO:0000313|EMBL:AAY95862.2};
GN Name=gltB {ECO:0000313|EMBL:AAY95862.2};
GN OrderedLocusNames=PFL_0453 {ECO:0000313|EMBL:AAY95862.2};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY95862.2, ECO:0000313|Proteomes:UP000008540};
RN [1] {ECO:0000313|EMBL:AAY95862.2, ECO:0000313|Proteomes:UP000008540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC {ECO:0000313|Proteomes:UP000008540};
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY95862.2; -; Genomic_DNA.
DR RefSeq; WP_011058827.1; NC_004129.6.
DR STRING; 220664.PFL_0453; -.
DR MEROPS; C44.003; -.
DR KEGG; pfl:PFL_0453; -.
DR PATRIC; fig|220664.5.peg.464; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_6; -.
DR Proteomes; UP000008540; 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:AAY95862.2}.
FT DOMAIN 15..405
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1482 AA; 162343 MW; 7B1E6C27433B1E42 CRC64;
MKAGLYQPDE FKDNCGFGLI AHMQGEPSHT LLKTAIEALT CMTHRGGINA DGKTGDGCGL
LMQKPDLFLR AVATEHFGIE LPKQYAVGMV FFNQDPVKAE AARENMNREI LAAGLQLVGW
RKVPIDTSVL GRLALERLPQ IEQVFIGGQG LSDQDFAIKL FSSRRRSSVA NAADTDHYIC
SFSHKTIIYK GLMMPADLAA FYPDLGDERL QTAICVFHQR FSTNTLPKWP LAQPFRFLAH
NGEINTITGN RNWAVARRTK FANDLIPDLE ELGPLVNRVG SDSSSMDNML ELMVTGGIDL
FRGVRMIIPP AWQNVETMDA DLRAFYEYNS MHMEPWDGPA GVVMTDGRYA VCLLDRNGLR
PARWVTTQNG FITLASEIGV WNYQPEDVIA KGRVGPGQIF AVDTETGQIL DTDAIDNRLK
SRHPYKQWLR KNALRIQATM EDNDHGSAFY DVDQLKQYMK MYQVTFEERD QVLRPLGEQG
YEAVGSMGDD TPMAVLSQRV RTPYDYFRQQ FAQVTNPPID PLREAIVMSL EICLGAERNI
FQESPEHASR VILSSPVISP AKWRSLMNLD RPGFERQVID LNYDESVGLE AAIRNVADQA
EEAARAGRTQ IVLSDRHIAP GKLPIHASLA TGAVHHRLTE KGLRCDSNIL VETATARDPH
HFAVLIGFGA SAVYPFLAYE VLGDLIRTGE VLGDLYEVFK NYRKGITKGL LKILSKMGIS
TIASYRGAQL FEAIGLSEEV CNLSFRGVPS RIKGARFVDI EAEQKALATE AWSPRKPIQQ
GGLLKFVHGG EYHAYNPDVV NTLQAAVQQG DYAKFKEYTA LVDNRPVSMI RDLFQVKTLD
TPMDISEVEP LESILKRFDS AGISLGALSP EAHEALAEAM NRLGARSNSG EGGEDPARYG
TIKSSKIKQV ATGRFGVTPE YLVNAEVLQI KVAQGAKPGE GGQLPGGKVN GLIAKLRYAV
PGVTLISPPP HHDIYSIEDL SQLIFDLKQV NPQALVSVKL VAEAGVGTIA AGVAKAYADL
ITISGYDGGT GASPLTSIKY AGAPWELGLA ETHQTLRGND LRGKVRVQTD GGLKTGLDVI
KAAILGAESF GFGTAPMIAL GCKYLRICHL NNCATGVATQ NEKLRKDHYI GTVDMVVNFF
TYVAEETREW LAKLGVRSLE QLIGRTDLLE VLEGQTAKQH HLDLTPLLGS DHIPADKPQF
CQVDRNPPFD KGLLAEKMVE MARSAINDKS GADFALDICN CDRSIGARIS GEIARLHGNQ
GMAQAPITFR FKGTAGQSFG VWNAGGLNLY LEGDANDYVG KGMTGGKLVI VPPKGSVYKT
QDSAIIGNTC LYGATGGKLF AAGTAGERFA VRNSGAHTVV EGTGDHCCEY MTGGFVCVLG
KTGYNFGSGM TGGFAYVLDQ DNTFVDRVNH ELVEIQRISG EAMEAYRSHL QRVLNEYVEE
TDSEWGRNLA ENLDDYLRRF WLVKPKAASL KSLLSSTRAN PQ
//
