UniProt: A0A1H7UH93

Database: UniProt
Entry: A0A1H7UH93_9SPHN

LinkDB:  A0A1H7UH93_9SPHN 
Original site:  A0A1H7UH93_9SPHN

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (8)   
   Pfam (4)   
   PROSITE (1)   
All databases (21)   

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ID   A0A1H7UH93_9SPHN        Unreviewed;      1508 AA.
AC   A0A1H7UH93;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   28-JAN-2026, entry version 25.
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   ORFNames=SAMN05216382_2986 {ECO:0000313|EMBL:SEL96018.1};
OS   Sphingomonas palmae.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Sphingomonadales; Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1855283 {ECO:0000313|EMBL:SEL96018.1, ECO:0000313|Proteomes:UP000199214};
RN   [1] {ECO:0000313|Proteomes:UP000199214}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS21-1 {ECO:0000313|Proteomes:UP000199214};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FNZZ01000007; SEL96018.1; -; Genomic_DNA.
DR   RefSeq; WP_093007751.1; NZ_FNZZ01000007.1.
DR   STRING; 1855283.SAMN05216382_2986; -.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000199214; Unassembled WGS sequence.
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:0019676; P:ammonia assimilation cycle; IEA:TreeGrafter.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
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; 3.20.20.70:FF:000097; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000199214}.
FT   DOMAIN          28..425
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   1508 AA;  163385 MW;  29456BF306D0CD30 CRC64;
     MSDAPMTDQR AWLAEHGMYR PEFEGDACGV GLVAATDGKP SRRVVQSAID ALKAVWHRGA
     VDADGKTGDG AGLHVDLPVR FFDDCVAASG HKLLPNRLAV GMVFLPRTDL GAQETCRTIV
     EAEMIEAGYT IYGWRQVPVD VSVIGAKAQL TRPEIEQIMI AGPLPDAVSA DEFEKNLYLV
     RRRIEKRVIA AQIQGFYVCS LSCRSIIYKG LFLAESLSVF YPDLTDQRFE SRVAIFHQRY
     STNTFPQWWL AQPFRCLAHN GEINTVRGNK NWMLSHEIRM ASIAFGEHSE DIKPVIPAGA
     SDTAALDATF EAICRSGRDA PTAKLMLVPE AWQAGGDTPD AHIAMYQYLA SVMEPWDGPA
     ALAMTDGRWA VGGVDRNALR PLRYTQTADG LLIIGSEAGM VVVPESTVVA KGRLGPGQMI
     AVDLLEGRVL RDREIKDKIA AEHDYAAMIG EFSAIDDLPP APADSTMRYD RAELARRQVA
     AGQTLEDMEL ILSPMVETAK EAIGSMGDDT PLAVISDKPR LISQFFRQNF SQVTNPPIDS
     LRERYVMSLK TRFGNLANIL DTEDRRERVL VLDSPVLTGA HWHRLKAYFG SSAAEIDCTF
     EAGGGAERLR AAIQRIRNQA EQAVREGRSE LFLTDEHIGE DRVAIPGVLA AAAVHTHLVR
     RGLRSYASVN VRTAECLDTH YYAVLIGVGA TTVNAYLAEA AIVDRQARGL FGDLSLDDCL
     VRHKKAIEEG LLKIMSKMGI SVLSSYRGGY NFEAVGLSRA LVNDLFPGMP AKISGEGYAS
     LHVNATERHE AAFDSAVATL PIGGFYRQRH TGEAHAYSAQ LMHLLQTAVS TDSYSSYLQF
     SRGVADLPPI YLRDLFQFNF PAEGVAVDQV EAITEIRKRF VTPGMSLGAL SPEAHETLAI
     AMNRIGAKAV SGEGGEDKIR YQPYENGDNA NSVIKQIASG RFGVTSEYLN ACEEIEIKVA
     QGAKPGEGGQ LPGFKVTEFI ARLRHSTPGV TLISPPPHHD IYSIEDLAQL IYDLKQINPR
     ARVCVKLVSS AGIGTVAAGV AKAHADVILV SGHVGGTGAS PQTSIKYAGT PWEMGLSEVN
     QVLTLNGLRG RIKLRADGGL KTGRDIVIAA ILGAEEFGIG TLSLVAMGCI MVRQCHSNTC
     PVGVCTQDPK LRDKFVGTPE KVINLMTFIA EEVRDILARL GVRSLDEVIG RTELLRQVSR
     GAEHLDDLDL NPILAKVDAT DAERRFSLST FRNEVPDSLD AQIIKDAAPV FSRGEKMQLT
     YSVRNTHRAV GTRLSSEVTR RFGMSKLADG HVTVRLRGSA GQSLGAFLCR GITLEVFGDA
     NDYVGKGLSG GTIIVRPAVS SPLASQDNTI LGNTVLYGAT AGRLLAAGQA GERFAVRNSG
     ADVVVEGCGA NGCEYMTGGT AVVLGEVGQN FGAGMTGGMA FVYDAAGRFA RNANPESIVW
     QRLASEHWEG KLRALVEAHA RATDSRWSKG LLEDWDAALA HFWQVVPKEM LTRLSYPLDD
     SVELVAAE
//

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