ID Q07YX4_SHEFN Unreviewed; 1482 AA.
AC Q07YX4;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Glutamate synthase (NADPH) large subunit {ECO:0000313|EMBL:ABI72790.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:ABI72790.1};
GN OrderedLocusNames=Sfri_2951 {ECO:0000313|EMBL:ABI72790.1};
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI72790.1, ECO:0000313|Proteomes:UP000000684};
RN [1] {ECO:0000313|EMBL:ABI72790.1, ECO:0000313|Proteomes:UP000000684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI72790.1,
RC ECO:0000313|Proteomes:UP000000684};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000447; ABI72790.1; -; Genomic_DNA.
DR RefSeq; WP_011638399.1; NC_008345.1.
DR STRING; 318167.Sfri_2951; -.
DR KEGG; sfr:Sfri_2951; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_6; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000000684; 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:ABI72790.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000684}.
FT DOMAIN 13..403
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1482 AA; 163033 MW; 38B0DCE90B977616 CRC64;
MSLYHPSFER DNCGFGLIAQ MDGDASHRIV RTAIHGLDRM KHRGGIAADG RTGDGCGLLM
QMPTDFFEAI AAENDWHLSR KFAVGMLFLS QDEQRADEAK FILEKELQRE TLSVAGWRKV
PINPDVLGEI GRESLPQIYQ VLINAPVGWR EKDLERRLYM ARRRLEQQIT DDKDFYVASL
SGQVIVYKGL MMPADLPSFY TDLADIRLKS AICLFHQRFS TNTSPKWPLA QPFRYLAHNG
EINTITGNRQ WARARAYKFN SPLLPDLQQA APFVNETGSD SSSLDNMLEM LLSGGMDLYR
AMRLLIPPAW QSNPEMDDEL KAFYDFNSMH MEPWDGPAGI VMTNGRHAAC AVDRNGLRPS
RYVITKDRIL TLASEVGIWD YSADEVIEKG RVGPGELLVL DTLNGRLYHS FEIDNDLKRR
HPYKEWMAKN SQTLIPAEEM APTKQGSSGF DSKTLLQYQK QFGFTREELE QVIWVLASKG
EEAIGSMGDD TPMAVLSKKS RSLYDYFRQK FAQVTNPPID PLREKHVMSL ATCVGREQNL
FSETTGNAYR VMFNSPILLF SDFNQLLGLD STNYRANTVD LNYDANETLE QAIRRITDEA
ERLARSGTTL LVLSDRAVAK SAQVIPAAMA VGSVQTRLVD KSLRCDTNII VETASARDPH
HFAVLIGFGA TAIYPYLAYE SISAMAKLHQ VDDVTHLMLN FRYGIEKGLR KIMSKMGIST
VGSYRCSQQF EAVGLASDVI ELCFKGVISR IEGVSFNHIA DDQKILHTAA YRAHVPLPQG
GLLKYVEGGE YHCFNPDVVN TLQASLKDKN YAEYKKFTHL VDDRPVATLR DLIGIKGQLN
AIEIDTVEGA EKLYPRFDSA AMSIGALSPE AHEALAVAMN RLGGRSNSGE GGEDARRFNS
ERNSAIKQIA SGRFGVTAHY LVNADVLQIK VAQGAKPGEG GQLPGHKVSV EIAGLRHARP
GVTLISPPPH HDIYSIEDLA QLIFDLKQIN PKALVSVKLV SEPGVGTIAT GVAKAYADMI
TISGYDGGTG ASPITSVKYA GSPWELGLAE VHQSLVENGL RHKIRLQVDG GLKTGTDVIK
AALLGAESFG FGTVPMIALG CKYLRICHLN NCATGVATQD KNLRENHYHG LPERVMTYFE
FVAQEVREWM AALGVTQFED LVGRSDWLHA LEGQTDKQRG LDLAPILYKP KVQANSSLTW
KEINPPSDVG QLNQTLLADC RKAVETGEPF SYQYQINNTD RSVGATLSGF IATTVGVTGA
KQPLTLGFNG SAGQSFGVWN SPGLELKLCG DANDYVGKGM SGGKIVIHPP IGSPFQSERS
AIMGNTCLYG ATGGKLFAAG QAGERFAVRN SGAIAVVEGS GDNCCEYMTS GIVVILGKTG
VNFGAGMTGG FAYVFDQFGR FNRRVNTEMV DTQKLESTIH QQHLKGLIET HYAETGSEHA
HMILSDFENW LDCFVLVKPK NIAVADLLKI EQKSPELVVK AG
//
