ID A0A1S3B4K5_CUCME Unreviewed; 1876 AA.
AC A0A1S3B4K5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN Name=LOC103485701 {ECO:0000313|RefSeq:XP_008441620.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008441620.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|RefSeq:XP_008441620.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + L-glutamine +
CC NADH; Xref=Rhea:RHEA:13753, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58359; EC=1.4.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00024267};
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 (NAD(+)
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00004944}.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC {ECO:0000256|ARBA:ARBA00004802}.
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
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DR RefSeq; XP_008441620.1; XM_008443398.2.
DR GeneID; 103485701; -.
DR OrthoDB; 20503at2759; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000089565; Unplaced.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
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; IPR006005; Glut_synth_ssu1.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR NCBIfam; TIGR01317; GOGAT_sm_gam; 1.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF14691; Fer4_20; 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 Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding 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:UP000089565}.
FT DOMAIN 1..175
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 691..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1846..1876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1854..1876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1876 AA; 205605 MW; 5361DACE6BEC6811 CRC64;
MRVLGHNGEI NTLRGNVNWM KAREGLLKCK ELGLSEDELK HLLPIVDASS SDSGAFDGVL
ELLIRAGRSL PEAVMMMIPE AWQNDKNMDP QRKALYEYFS CLMEPWDGPA LISFTDGRYL
GATLDRNGLR PGRFYVTHSG RVIMASEVGV VDIAPEDVSR KGRLNPGMML LVDFENHVVV
DDEALKQQYS LARPYGEWLK NQKIELKDVI GSIDKSEMTT PAITGALSAE DNMNNMGIHG
LLTPLKAFGY TTEALEMLLL PMAKDGVEAL GSMGNDTPLA VMSNREKLTF EYFKQMFAQV
TNPPIDPIRE KIVTSMQCMI GPEGDLTETT EEQCHRLSLK GPLLSIGEME AIKKMNYRGW
RSKVLDITYP KYLGRRGLEE TLDRICSEAQ NAIQEGFTTL VLSDRAFSSK RVAVSSLLAV
GAVHQYLVKN LERTQVGLIV ESAEPREVHH FCTLVGFGAD AICPYLAIEA IWRLQIDGKI
PAKSSGEFHT KEELVKKYFK ASNYGMMKVL AKMGISTLAS YKGAQIFEAL GLSSEVVEKC
FAGTPSRVEG ATFEMLARDA HNLHEMAFPS RAFPPGSAEA VALPNPGDYH WRKGGEIHLN
DPVAMAKLQE AARTNSVNAY KEYSKLVHEL NKACNLRGLL KFKETGASIP LDEVEPASEI
VKRFCTGAMS YGSISLEAHT TLAMAMNKIG GKSNTGEGGE QPSRMEPLPD GSMNPKRSSI
KQVASGRFGV SMYYLTNADE LQIKMAQGAK PGEGGELPGH KVVGEIAKTR NSTAGVGLIS
PPPHHDIYSI EDLAQLIHDL KNSNPAARIS VKLVSEAGVG VIASGVVKGH ADHVLISGHD
GGTGASRWTG IKNAGLPWEL GLAETHQTLV ANDLRGRTVL QTDGQLKTGR DVAMAALLGA
EEFGFSTAPL ITMGCIMMRK CHKNTCPVGI ATQDPVLREK FAGEPEHVIN FFFMVAEEMR
EIMSQLGFRT VNQMVGRSDV LEVDKEVAWQ NEKLENIDLS LLLRPAADLR PEAAQYCVQK
QDHGLDMALD QKLIALSKSA LEKSIPVYIE TPIINVNRAV GTMLSHEVTK RYHMAGLPSE
TIHIKFTGSA GQSLGAFLCP GIMLELEGDS NDYVGKGLSG GKIVVYPPKG SLFDPKENII
IGNVALYGAT SGEAYFNGMA AERFCVRNSG AKAVVEGVGD HGCEYMTGGT VVILGKTGRN
FAAGMSGGIA YVLDMDGKFE SRCNLELVDL DKVEEEDDIL TLKMMIQQHQ RHTSSNLAKE
VLDNFENLLP RFIKVFPREY KRILADMKAQ EAVKEALEPS AKDAEESDEA ELVEKDAFEE
LKKMAAASLN GNSEQVEKTE PPKRPTEIPD AVKHRGFIAY EREGVKYRDP NVRMRDWKEV
MEESKPGPLL KTQSARCMDC GTPFCHQENS GCPLGNKIPE FNELVYQNRW REALERLLET
NNFPEFTGRV CPAPCEGSCV LGIIENPVSI KNIECAIIDK AFEEGWMIPR PPQVRSGKRV
AIVGSGPAGL AAADQLNKMG HKVTVYERAD RIGGLMMYGV PNMKTDKVDV VQRRVNLMAE
EGVNFVVNAN VGTDTSYSLD QLRKENDALV LAVGATKPRD LPVPGRELAG VHFAMEFLHS
NTKSLLDSNL QDGNYISAKD KKVVVIGGGD TGTDCIGTSI RHGCSSIVNL ELLPQPPQTR
APGNPWPQWP RIFRVDYGHQ EAAAKFGKDP RTYEVLTKRF IGDENGVVKG LEVIRVQWEK
DADGRFQFKE VEGSEEIIEA DLVLLAMGFL GPESTVAEKL GIEKDNRSNF KAEYGRFSTS
VDGVFAAGDC RRGQSLVVWA ISEGRQAAAQ VDKYLAKEEK GGIVGEGGYE GVGNGSQDYN
NRQQDSSSSS RHTVMT
//
