ID A0A0Q5C7L4_9MICO Unreviewed; 1523 AA.
AC A0A0Q5C7L4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KQQ27474.1};
GN ORFNames=ASF54_01335 {ECO:0000313|EMBL:KQQ27474.1};
OS Frondihabitans sp. Leaf304.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=1736329 {ECO:0000313|EMBL:KQQ27474.1, ECO:0000313|Proteomes:UP000051456};
RN [1] {ECO:0000313|EMBL:KQQ27474.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ27474.1,
RC ECO:0000313|Proteomes:UP000051456};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ27474.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ27474.1,
RC ECO:0000313|Proteomes:UP000051456};
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=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}.
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:KQQ27474.1}.
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DR EMBL; LMNV01000002; KQQ27474.1; -; Genomic_DNA.
DR RefSeq; WP_055957849.1; NZ_LMNV01000002.1.
DR STRING; 1736329.ASF54_01335; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000051456; Unassembled WGS sequence.
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: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 Reference proteome {ECO:0000313|Proteomes:UP000051456}.
FT DOMAIN 29..418
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1523 AA; 164960 MW; FD62522FD69B242C CRC64;
MALTPAHQTF STIPAAQGLY DPAQEKDACG LAMVATLRGT PGHDIIDAAL GALRNLEHRG
AVGSDAGTGD GAGILMQVPD AFFREVVEFD LPEAGHYAVG IAFLPTDFDE RKTLQAAIEK
IVVEESLRVV GWRDVPVRSG ELGTLARNAM PAFEQLFVAA AHGSDHVEGV ALDRLAFRMR
KRAERELGAY FTSLSSRTMV YKGMVTTLQL EPFYPDLSDE RVASKLAIVH SRYSTNTFPS
WPLAQPFRMI AHNGEINTVR GNRNWMRARQ SQLESELIGD VTPLLPIVTP GNSDSASFDE
VVELLSLTGR SLPHAIMMMV PEAWENQVGI DPVLRDFYEY HSMLMEAWDG PAAITFTDGS
LAGATLDRNG LRPGRYLVTD DGLVVLASEI GVLPDIDQSK IVRKGRLRPG KMFLVDTEAG
RIIEDDEIKQ QLASSEEYGE WLEMGRIHLK DLPEREHIVH TPASVTRRQR TFGYTEEEVR
ILLTPMAKAG AEPLGAMGSD TPIAVLSDRP RLLFDYFTQQ FAQVTNPPLD SIRESVVTSL
KLGLGPERNL LDATPEHARQ VILDFPVIDN DELAKIQHID PAPGSRLTAT LRGLYRVDQG
PRAMEDRIAA LCAEVDEAIA EGSEFIVLSD RDSTAEFAPI PSLLMLAAVH HHLIRTENRM
KVGLIVEAGD VREVHHVATL IGYGASAINP YLAMETCENL VRSGMITGMS PEQAVKNVIK
ALGKGVLKIM SKMGISTVSS YAAAQAFEAV GLSQEFIDTY FTGTSTRLGG VGVDVIAAEN
AERHLSAYPA DGASPAHERL QTGGEYQWRR EGPPHLFNPE TVFRLQHATR TRRYDIFREY
TKMVDDQAEQ LMTLRGLFTL RTHARPTVPL DEVESVESIV KRFSTGAMSY GSISKEAHET
LAIAMNRLGG KSNTGEGGED VDRLLDPERR SAVKQVASGR FGVTSMYLTH ATDIQLKMAQ
GAKPGEGGQL PPSKVYPWVA RTRHATPGVG LISPPPHHDI YSIEDLKQLI FDVKRANPTA
RVHVKLVSQS GIGAVAAGVT KALADVVLVS GHDGGTGASP LNSLKHAGTP WEIGLAETQQ
TLMMNGMRDR VVVQVDGQMK TGRDVIVAAL LGGEEFGFAT APLVVSGCIL MRVCHLDTCP
VGVATQNPEL RARFTGKAEH VVNFFEFLAQ EVREYLSELG FRSLDEAIGH HELLGVDRAI
DHWKASGLDL SPVLVGPVFA DDEPRRNFVQ QDHELEKHFD NQLIAASADV IATGGSIALD
LPIRNTERAV GTMLGHEVTV QRGEHGLPAG SIDITLRGSA GQSLGAFLPA GITLRLVGDS
NDYVGKGLSG GTVIVRPPEE ASFPAEDNVI AGNVIGYGAT QGSMFIRGIV GERFLVRNSG
ASAVVEGVGD HALEYMTGGL AVILGETGRN LGAGMSGGTA YVRGLRRENV NDDSLTAGEL
LLQPLGSADI EILEDLLQQH LAETGSPVAE KLLVDIEKSA EEFVKVLPRD YAAVMETRKT
AAAEGLDLDG DEVWNRIMEV TGG
//
