ID A0A0W7WIR7_9RHOB Unreviewed; 1511 AA.
AC A0A0W7WIR7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:KUF10477.1};
GN ORFNames=AVJ23_11360 {ECO:0000313|EMBL:KUF10477.1};
OS Pseudoponticoccus marisrubri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudoponticoccus.
OX NCBI_TaxID=1685382 {ECO:0000313|EMBL:KUF10477.1, ECO:0000313|Proteomes:UP000054396};
RN [1] {ECO:0000313|EMBL:KUF10477.1, ECO:0000313|Proteomes:UP000054396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJ5A-1 {ECO:0000313|EMBL:KUF10477.1,
RC ECO:0000313|Proteomes:UP000054396};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-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:KUF10477.1}.
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DR EMBL; LPXO01000006; KUF10477.1; -; Genomic_DNA.
DR RefSeq; WP_058862317.1; NZ_LPXO01000006.1.
DR STRING; 1685382.AVJ23_11360; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000054396; 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:UP000054396}.
FT DOMAIN 34..431
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 909..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1511 AA; 164654 MW; 1616366284595945 CRC64;
MTKFDTDWAR AEETKRKWMS ENGLYHESEE HSSCGVGLTV SLDGKPSRSV VEAGITALKA
IWHRGAVDAD GMTGDGAGIH VQIPVPFFYD QIQRTGHDPR KDELIAVGQV FLPRTDFGAQ
EACRTIVETE VLRMGHYIYG WRHVPVNVDC LGEKANATRP EIEQILISNA KGVDEETFER
ELYVIRRRIE KAAGAAGITG LYIASLSCRS IIYKGMMLAE QVSEFYPDLQ DERFESSFAI
YHQRYSTNTF PQWWLAQPFR MLAHNGEINT LKGNTNWMKS HEIRMAHAAF GDMAEDIKPI
IANGSSDSAA LDSVFEVLVR AGRNAPMAKT MLVPESWSKQ AVELPQSWRD MYSYCNSVME
PWDGPAALAM TDGRWVCGGL DRNGLRPMRY VVTGDGMLIA GSEVGMVPTD EATVREKGAL
GPGQMIAVDM KEGKLYHDVE IKDRLASALP FGEWVGKITE LDEPLAALTE TPLFDGAELR
RRQIAAGYTI EELESVLSPM VEDAKEVVAS MGDDTPSAVL SKRYRPLSHY FRQNFSQVTN
PPIDSLREFR VMSLKTRFGN LKNVLDESSA QTEILVLDTP FVGNAQFEAL KEHFNAPCTE
IDCTFAPGEG ALRLGLERIR SEAEDAVRSG AGHIILTDEH CGPDRVAMPM ILATSAVHSH
LTRKGLRTFC SLNVRAAECI DPHYFAVLIG AGATIVNPYL AEDSLADRIG RGLLEMDLTT
AMARYREAID QGLLKIMSKM GISVISSYRG GLNFEAVGLS RAMCAEYFPG MISRISGIGV
SGIQKKAEEI HALGFRGGRD VLPIGGFYKM RKSGETHAWG AQVMHLMQAA CDRASFEMWK
QYSNAMQANP PIHLRDLLAI KPLGKSIPIE EVESITSIRK RFVTPGMSLG ALSPEAHKTL
NVAMNRIGAK SDSGEGGEDP AHFVPEPNGD NPSAKIKQVA SGRFGVTAEY LNHCEELEIK
VAQGAKPGEG GQLPGMKVTD LIARLRHSTK GVTLISPPPH HDIYSIEDLA QLIYDLKQIN
PTVKVTVKLV ASSGVGTIAA GVAKAEADVI LISGHNGGTG ASPATSIKYA GLPWEMGLTE
AHQVLAMNNL RDRVVLRTDG GLRTGRDIVM AAMLGAEEYG IGTAALIAMG CIMVRQCQSN
TCPVGVCTQD EALRAKFTGN ADKVVNLITF YAQEVREILA EIGARSLDEV IGRADLLSQV
SRGAEHLDDL DLNPLLIRVD GSDEIEYNRD RPRNPVRDTL DAEIVRDAAR FLQDGEKMQL
SYAVMNTHRT VGTRVSSHIV RKFGMRNALQ PDHLHVKLTG SAGQSLGAFA APGLKLEVSG
DANDYVGKGL SGGLIVVRPP LVSPLAASEN TIIGNTVLYG ATDGHLFAAG KAGERFAVRN
SGARVVVEGC GSNGCEYMTG GVAVILGRIG ANFGAGMTGG MAYLYDPEGQ APDMMNMESL
VTCKVTTPEW EAELKGLIER HFAETKSRKA EDILQNWDIE KDNFLQVCPR EMLDKIPHPL
GIEDDLAVPA E
//
