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
//