ID A0A0Q8MUT3_9CAUL Unreviewed; 593 AA.
AC A0A0Q8MUT3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KRB49416.1};
GN ORFNames=ASE02_16460 {ECO:0000313|EMBL:KRB49416.1};
OS Phenylobacterium sp. Root700.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=1736591 {ECO:0000313|EMBL:KRB49416.1, ECO:0000313|Proteomes:UP000051042};
RN [1] {ECO:0000313|EMBL:KRB49416.1, ECO:0000313|Proteomes:UP000051042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root700 {ECO:0000313|EMBL:KRB49416.1,
RC ECO:0000313|Proteomes:UP000051042};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB49416.1, ECO:0000313|Proteomes:UP000051042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root700 {ECO:0000313|EMBL:KRB49416.1,
RC ECO:0000313|Proteomes:UP000051042};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRB49416.1}.
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DR EMBL; LMHT01000011; KRB49416.1; -; Genomic_DNA.
DR RefSeq; WP_056732199.1; NZ_LMHT01000011.1.
DR AlphaFoldDB; A0A0Q8MUT3; -.
DR STRING; 1736591.ASE02_16460; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000051042; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.70.3270; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 492..521
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 551..581
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 593 AA; 65386 MW; DF8793E3119F2433 CRC64;
MQRTSTEGPD YFHKVVDCQW ACPAHTPVPE YIRLIAEGRY SDAYMVNWKS NVFPGILGRT
CDRPCEPACR RGRVEDEPVA ICRLKRVAAD NKEDITGRLP VPVAVSNGKR IALVGAGPAS
LTVARDLAPL GYELTLFDGE AKAGGMIRSQ IPRFRLPEEV IDEEVGYITG LGMEVRLGQR
IDSLKALLTE DYDAVFIGSG APRGRDLDLP GRQEAAANIH IGIDWLSNVS FEHVDKIGKR
VIVLGGGNTA MDCCRTSRRL GGEDVKVIVR SGFDEMKASP WEKEDAIHED IPILNYLVPK
AFTHENGKLT GVTFEKVRPE FDDKGRRKLV ASGEPDQHFE CDDVLVAVGQ ENAFPWIERD
VGIEFDEWGM PKVDTLTFQS TLPSVFFGGD AAFGPKNIIW AVAHGHDAAI SIDKLCKAED
LTARPPPGFS MASQKMGIHE WSYDNDPAND GRYKVPLREK AQALKDVRLE VELGFAREMA
YRETQRCLNC DVQTVFAESA CIECDACADI CPVDCITFTD NGEEDDLRGR LSAPALNADQ
ALMVSGELKT GRVMVKDEDV CLHCGLCAER CPTGAWDMQK FLLDMTHAGG SCR
//
