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Database: UniProt
Entry: A0A229FY90_9BURK
LinkDB: A0A229FY90_9BURK
Original site: A0A229FY90_9BURK 
ID   A0A229FY90_9BURK        Unreviewed;      1587 AA.
AC   A0A229FY90;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:OXL16538.1};
GN   ORFNames=AOC33_02595 {ECO:0000313|EMBL:OXL16538.1};
OS   Polynucleobacter cosmopolitanus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=351345 {ECO:0000313|EMBL:OXL16538.1, ECO:0000313|Proteomes:UP000215188};
RN   [1] {ECO:0000313|EMBL:OXL16538.1, ECO:0000313|Proteomes:UP000215188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWH-MoIso2 {ECO:0000313|EMBL:OXL16538.1,
RC   ECO:0000313|Proteomes:UP000215188};
RA   Hahn M.W.;
RT   "Reclassification of a Polynucleobacter cosmopolitanus strain isolated from
RT   tropical Lake Victoria as Polynucleobacter victoriensis comb. nov.";
RL   Submitted (JUN-2017) 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:OXL16538.1}.
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DR   EMBL; NJGG01000001; OXL16538.1; -; Genomic_DNA.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000215188; 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}.
FT   DOMAIN          29..429
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   1587 AA;  172966 MW;  6ACFA69907AFE54A CRC64;
     MKEISVTTTP SLRPEAQGLY DPVNEHDACG VGFVAHIKGH KSHDIVSQGL KILENIDHRG
     AVGADPLMGD GAGILIQIPD QFYREEMAKQ GVNLPPAGEY GVGMVFMPKE SASRLACEQE
     LERTVRIEGQ VVLGWRNVPV DANMPMSPTV RKTEPVIRQI FIGRGRDIMT TDALERKLYV
     IRKTGSHAIQ ALQLQHGKEY FVTSMSARTV VYKGLLLANQ VGAYYEDLKD SRVVSALALV
     HQRFSTNTFP AWELAHPYRM IAHNGEINTV KGNVNWINAR TGAISSPVLG DDLQKLWPLI
     YPGQSDTASF DNCLELLVMA GYPMAHAMMM MIPEAWEQHT LMDDNRRAFY EYHAAMMEPW
     DGPAAIAFTD GRQIGATLDR NGLRPARYYV TDDDLVIMAS EAGVLTFPEN KIIKKWRLQP
     GKMFLIDMEQ GRIIDDVELK DALAKAKPYK SWIEAVRIKL DEIDASAADL KDDAEKIRPA
     ASLLDRQQAF GYTQEDLKFL MAPMASSGEE AIGSMGNDSP LAVLSNKNKP LYNYFKQLFA
     QVTNPPIDPI RENMVMSLVS FVGPKPNLLD TNNINPPMRL EVSQPILDFD DIAKVRHIEH
     YTGGKFRSYE LDICYPSVWG KDGVEARLAS LCAEAVDAVH SGYNILIISD RQVAADHVAI
     PALLATSAIH QHLVDKGLRT STGLVVETGS ARETHHFALL AGYGAEAVHP YLAMETLVDM
     AKGLKGDLSA EKVVKNFTKA VGKGLQKVMS KMGISTYMSY TGAQIFEAIG LNKELIDKYF
     KGTASNVGGI GIFEVAEEAL KMHSLAFGND PTLTNMLDAG GEYAFRVRGE DHMWTPDSIA
     KLQHSTRQGP EKGGYQTYKE YANIINDQTK RHMTLRGLFE FKIDPNKAIP LDEVESAKEI
     VKRFATGAMS LGSISTEAHA TLAIAMNRIG GKSNTGEGGE DNKRYRNELK GIAIKSGETL
     ASILGDDVIE ANIPLSDGDS LRSKIKQVAS GRFGVTAEYL TSADQIQIKM AQGAKPGEGG
     QLPGSKVSDY IGKLRYSVPG VGLISPPPHH DIYSIEDLAQ LIHDLKNVNS KADISVKLVS
     EVGVGTVAAG VAKAKADHVV IAGHDGGTGA SPLSSIKHAG SPWELGLAET QQTLVLNGLR
     SRIRVQADGQ MKTGRDVVIG ALLGADEFGF ATAPLVVEGC IMMRKCHLNT CPVGVATQDP
     ELRKKFSGKP EHVVNFFFFI AEEAREIMAQ LGIRKFDDLI GHTELLDTKK SIEHWKARGL
     DFSKIFQAPN VPASVPKFQV ETQDHGLSTA LDHALIEKSK AALEKGERVS FIQPIKNVNR
     TAGAMLSGEV AKRYGHEGLP DDTIHIQLNG TAGQSFAAFL AHGVTMDLVG DGNDYVGKGL
     SGGRVIVRAP HEFRGDTSQN IIVGNTVLYG AIAGEAFFNG VAGERFAVRN SGAIAVVEGT
     GDHGCEYMTG GTVVALGLTG RNFAAGMSGG IAYVYDEDGL FAKRCNTSMA TLEPVLSSAE
     QEAKMPKPEW HALVNVKEGG ERLTDEVILK NLIERHFKHT GSERAKAILA DWDKSRARFV
     KVFPTEYKRA LGELWEKSQG NKQAASV
//
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