ID A0A243PHW9_9SPHN Unreviewed; 1512 AA.
AC A0A243PHW9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:OUC56251.1};
GN ORFNames=CA262_16385 {ECO:0000313|EMBL:OUC56251.1};
OS Sphingobium sp. GW456-12-10-14-TSB1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1987165 {ECO:0000313|EMBL:OUC56251.1, ECO:0000313|Proteomes:UP000194660};
RN [1] {ECO:0000313|EMBL:OUC56251.1, ECO:0000313|Proteomes:UP000194660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW456-12-10-14-TSB1 {ECO:0000313|EMBL:OUC56251.1};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-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:OUC56251.1}.
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DR EMBL; NGUN01000003; OUC56251.1; -; Genomic_DNA.
DR RefSeq; WP_017181740.1; NZ_NGUN01000003.1.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000194660; 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 31..429
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1512 AA; 164632 MW; 99A9870FDC8BBB40 CRC64;
MTDTPFTASP EERARIAAEG MYHPDLEGDA CGVGLVAATD GRPSRRVVAS AIDALKAVWH
RGAVDADGKT GDGAGIHVDL PVRFFDDAIA DSGHKPLPNR LAVGMIFLPR TDLSAQETCR
TIVESEIIDA GYTIYGWRQV PVDVSVIGEK AQRTRPEIEQ IMIAGPMPEV RDQAEFEKDL
YLIRRRIEKQ VIAAQINDFY ICSLSCRSII YKGLFLAESL SVFYPDLQDE RFESRVAIFH
QRYSTNTFPQ WWLAQPFRTL AHNGEINTIR GNKNWMKSHE IKMASLAFGE QSEDIKPVIP
AGASDTAALD AVFEAICRSG RDAPTAKLML VPEAWQADNG ELPKAHRDMY DYLASVMEPW
DGPAALAMTD GRWVVAGVDR NALRPLRYTL TGDNLLIVGS ETGMVVVPET TIVRKGRMGP
GQMIAIDLAE GEIYDDAAIK NRIAGERPYG DLIKDFMAIG DLTDAPTALP DWDKAELTRR
QVAANLTLED LELILAPMVE DAKEAIGSMG DDTPLAVISD KPRTISHFFR QNFSQVTNPP
IDPLRERHVM SLKTRFSNLH NILEQDAQNS HVLVLESPVL TSAEWARLKA HFGPAVAEID
CTFPANGGQE QLRAAIARIR EEAEQAVREG RTEIFLTDEG VSETRIAIAG VLAAAAVHTH
LVRKGLRSYA SINVRCAEAL DTHYFAVLIG VGATTVNAYL AEASIADRHA RGLFGSLDLD
ACFERYRVAV NEGLLKIMSK MGIAVISSYR GGYNFEAVGL SRALVNDLFP GMPAKISGEG
YASLHYSAIL RHQQAYDASV VRLPIGGFYR QRNGGEAHAY SAQLMHLLQT AVATDSYSTY
LQFSRGVRDL PPVYLRDLME FNFAREAVPI DEVEATTEIR KRFVTPGMSL GALSPEAHET
LAIAMNRIGA KAVSGEGGED AARFKPYENG DNANSVIKQI ASGRFGVHAE YLASAEEIEI
KVAQGAKPGE GGQLPGFKVT EFIARLRHST PGVTLISPPP HHDIYSIEDL AQLIYDCKQI
NPRARVCVKL VSQAGIGTVA AGVAKAHADV ILIAGHVGGT GASPQTSIKY AGTPWEMGLS
EANQVLTLNG LRHRVKLRTD GGLKTGRDIV IAAILGAEEY GIGTLSLVAM GCIMVRQCHS
NTCPVGVCVQ DEKLRAKFTG TPEKVINLMT FIAEEVREVL ARLGFRSLDE VIGRTELLKQ
VNRGAEHLDD LDLNPILAKV DAPDDQRRFS LKQWRNDVPD SLDAQMMRDA KAVFERGEKM
QLTYTVRNTH RAVGTRLSSA VTDKFGMSAL ADGHLTVRLR GSAGQSLGAF LCKGITLEIF
GDANDYVGKG LSGGIITVRT TVSSPLSSKD NTIIGNTVLY GATSGKLFAA GQAGERFAVR
NSGAQVVVEG CGANGCEYMT GGIAVILGKT GANFGAGMTG GMAFILDEDG SFTSRANPEG
IVWQRLESAH WEAQVKDLIA QHAKATDSKW SSTILEDWDR WRRYIWQVCP KEMISRLTHP
LSDAPAEVVA AE
//
