ID A0A511DE50_9PSEU Unreviewed; 1522 AA.
AC A0A511DE50;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 18-JUN-2025, entry version 22.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:GEL22683.1};
GN Name=gltB {ECO:0000313|EMBL:GEL22683.1};
GN ORFNames=PSU4_16370 {ECO:0000313|EMBL:GEL22683.1};
OS Pseudonocardia sulfidoxydans NBRC 16205.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1223511 {ECO:0000313|EMBL:GEL22683.1, ECO:0000313|Proteomes:UP000321685};
RN [1] {ECO:0000313|EMBL:GEL22683.1, ECO:0000313|Proteomes:UP000321685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16205 {ECO:0000313|EMBL:GEL22683.1,
RC ECO:0000313|Proteomes:UP000321685};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Pseudonocardia sulfidoxydans NBRC
RT 16205.";
RL Submitted (JUL-2019) 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:GEL22683.1}.
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DR EMBL; BJVJ01000011; GEL22683.1; -; Genomic_DNA.
DR RefSeq; WP_147104396.1; NZ_BJVJ01000011.1.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000321685; 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:0019676; P:ammonia assimilation cycle; IEA:TreeGrafter.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00982; gltB_C; 1.
DR CDD; cd00713; GltS; 1.
DR CDD; cd02808; GltS_FMN; 1.
DR FunFam; 3.20.20.70:FF:000031; Glutamate synthase 1 [NADH]; 1.
DR FunFam; 3.20.20.70:FF:000053; Glutamate synthase large subunit; 1.
DR FunFam; 2.160.20.60:FF:000001; Glutamate synthase, large subunit; 1.
DR FunFam; 3.60.20.10:FF:000001; Glutamate synthase, large subunit; 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; IPR050711; ET-N_metabolism_enzyme.
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 InterPro; IPR001202; WW_dom.
DR NCBIfam; NF008730; PRK11750.1; 1.
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.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
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:UP000321685}.
FT DOMAIN 28..421
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 322..357
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1522 AA; 164951 MW; 6C5FFB565625A073 CRC64;
MAAISEQTGG PEGRSGGLYS PDHEHDACGV ALVADLKGRR DHGIVRKGLT ALLRLEHRGA
RGAETNTGDG AGILIQVPDE FFRAVVDFDL PQPGAYAVGT AFLPADPAKA DEAVARIDAL
AAEENLRVLG WRELPTDPDG ADIGPSARAS MPGFRQLFVA GSEPAAAEAP TGIELERRTF
CLRKRVEHTV GVYFPSLSPR TIVYKGMLAE PQVEAFYPDL SDERVTSALA VVHSRFSTNT
FPAWPLAHPY RYVAHNGEIN TLRGNRNWMA AREALLASDV LPGDMERLTP VVTPDASDSA
TFDEVLELLH LGGRSLPHAV LMMIPEAWEN HTEMDPARRA FYEYHSTLME PWDGPALVAF
TDGTVIGAVL DRNGLRPARY WVTEDGLVVL ASEVGVLDVP ASQVVRKGRL EPGRMFLVDT
AAGKIVDDDE IKGELAAEHP YEEWLHSGLI RLEELPDRER EQIAHSALQH RQQTFGYTEE
ELTVLLRPMA MTGAEPIGSM GNDAPIAGIS ERPRQLYDYF IQLFAQVTNP PLDAIREELV
TSLQSQLGPE QNLLQAGPAS CRTIVLPFPV LGNDDLARIV HINDDGEYPG FASHTVRGLF
EAAKGGDGLV ERLEEIKAEV SQAIADGAHL IVLSQRGVDA THAPIPSLLL TGAVHHHLVR
ERTRTRVGLV VEAADAREVH HIALLIGYGA AAVNPYLAMA TVEDLADRGD IPGVDAKTAA
KNLVKALGKG VRKTMSKIGV STVASYTGAQ IFESIGLGHE VIDSCFTGTT SRLGGVGFDV
LAEEVLRMHR KAFPRDDVRA THRTLESGGE YQWRREGELH LFNPQTVFKL QHSTRQGRYD
VFKEYTRAVD DQAGRLMTLR GLFKLKEGVR PPVPIDEVEP VESIVTRFAT GAISYGSISQ
EMHQTLAIAM NRLGGKSNTG EGGEDTDRFT PDANGDSRRS AVKQVASGRF GVTSEYLVNS
DDIQIKIAQG AKPGEGGQLP GSKVYPWIAK TRYSTPGVGL ISPPPHHDIY SIEDIKQLIH
DLKNANPRAR IHVKLVSQVG VGTVAAGVAK AHSDVVLISG HDGGTGASPL SSIKHAGGPW
ELGLAETQQT LIANNLRDRI VVQADGQMKT GRDVVIAALL GAEEFGFATA PLVVSGCIMM
RVCHLDTCPV GVATQNPVLR ERFDGKAEYV VNFMRFIAEE VREYLAALGF RTLEEAVGHA
EMLDTDDAVR HWKTQGLDLR PIFYMPKPPA GSSRHRTRGQ DHGLEKALDN TVIQLAEGAL
ASGDKVRLDL PVRNVNRTVG TMLGYELTKR WGGEGLPDDT IDITFTGSAG QSFGAFVPRG
ITMRLVGDTN DFFGKGLSGG RLTLRPDPTA PFTAEENVIA GNVILYGATS GEIFVRGIVG
ERFCVRNSGA TAVVEGVGDH GCEYMTGGKA VVLGRVGRNF AAGMSGGVAY VLDLPQHRVN
PEMVDIDPLD EADREFLRDI VERHHAETDS AVARALLTDW DVAVERFGKV MPKDYKRVLK
ARAAAERDGR NVDEAIMEAS HG
//
