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Database: UniProt
Entry: A0A1I5E6T4_PARPN
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Original site: A0A1I5E6T4_PARPN 
ID   A0A1I5E6T4_PARPN        Unreviewed;      1516 AA.
AC   A0A1I5E6T4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Glutamate synthase (NADPH) large subunit {ECO:0000313|EMBL:RKS52691.1};
GN   ORFNames=BDE18_2023 {ECO:0000313|EMBL:RKS52691.1};
OS   Paracoccus pantotrophus (Thiosphaera pantotropha).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=82367 {ECO:0000313|EMBL:RKS52691.1, ECO:0000313|Proteomes:UP000273626};
RN   [1] {ECO:0000313|EMBL:RKS52691.1, ECO:0000313|Proteomes:UP000273626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35512 / DSM 2944 / CIP 106514 / LMD 82.5 / NBRC 102493 /
RC   NCCB 82005 / GB17 {ECO:0000313|Proteomes:UP000273626};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC       {ECO:0000256|ARBA:ARBA00004802}.
CC   -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
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:RKS52691.1}.
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DR   EMBL; RBLI01000001; RKS52691.1; -; Genomic_DNA.
DR   Proteomes; UP000273626; 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; GLUTAMINE AMIDOTRANSFERASE TYPE-2 DOMAIN-CONTAINING PROTEIN; 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          35..432
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   REGION          912..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1516 AA;  165605 MW;  E9F6A73CE8131EAF CRC64;
     MKDCEQMSWE QQEQARRDWM AEHSLYRAED EHSSCGVGLV VSIDGKASRK VVESGITALK
     AIWHRGAVDA DGKTGDGAGI HVQIPVPFFY DQVRRTGHEP DHDKLIAVGQ VFLPRTDFAA
     QERCRTIVES EVLRMGHYIY GWRHVPVNTA VLGEKANATR PEIEQILIRC DKDIDDEQFE
     RELYIIRRRI EKAAVAAQIA GMYICTLSCR SIIYKGMMLA EQVAEFYPDL KDERFESAFA
     IYHQRYSTNT FPQWWLAQPF RMLAHNGEIN TLKGNSNWMK SHEIRMASRT FGEMAEDIKP
     IIPGGSSDSA ALDAVFEVLV RSGRNAPMTK TILVPEAWSK ATTDMPKAWA DMYAYCNSIM
     EPWDGPAALA MTDGRWVCGG LDRNGLRPLR YVVTGDNLLI AGSEAGMVPV NETAVREKGA
     LGPGQMIAVD MAEGKLYHDR EIKDHLAASQ PFGDWVEKVV QPSELMAKLP ETALHSGEEL
     HRRQIAVGYT VELVEQMLVP MAEDAKEALA SMGDDTPPAV LSRQFRPLSH YFRQNFSQVT
     NPPIDSLRES RVMSLRTRFG NLKNVLEESS THAEITMLES PFLANGEFEE LTRMFQGQAT
     QIDCTFPANG GPDALAEALA RIRAEAEDAV RSGNGHIILT DEGISANRVG VPMILATSAV
     HSWLTRKGLR TFCSLNVRAS ECVDPHDFAV LIGCGATTVN PYLAQDTLAE RIERGLLDGN
     LIDIMTRYRE AIDAGLLKIM AKMGISVLSS YRGGLNFEAV GLSRAMVAEY FPGMQSRISG
     IGLHGLQAKL EEAHAKGFRA PLVDLLPVGG FYKARRSGEK HAWEANTMRL LQLACEKASY
     DVWKQFTATM RANPPIHIRD LLDIKPLGKP VPLEEVESIT SIRKRFVTPG MSLGALSPEA
     HMTLNIAMNR IGAKSDSGEG GEDPAHSHPL PNGDNPCAKI KQVASGRFGV TAEYLNACEE
     LEIKVAQGAK PGEGGQLPGM KVTDLIARLR HSTKGVTLIS PPPHHDIYSI EDLAQLIYDL
     KQINPRAKIT VKLVASSGVG TIAAGVAKAK ADVILISGHN GGTGASPATS IKFAGLPWEM
     GLTEAHQVLA MNRLRDRVTL RTDGGLRTGR DIVMAAMMGA EEYGIGTAAL IAMGCIMVRQ
     CQSNTCPVGV CTQDEKLRAM FNGSADKVVN LITFYATEVR EILASIGARS LDEVIGRADL
     LTQVSRGDKS LDDLDLNPLL ITVDGSEKIV YDRSKPRNAV PDTLDAEIIR DAGRFFSDGE
     KMQLSYAVRN TQRTVGTRTS SMIVQTFGMR NKLQPDHLTV RLTGSAGQSL GAFAAPGLKI
     EVSGDANDYV GKGLSGGTIV VRPPMGSPLK AAENTIIGNT VLYGATDGYL FAAGRAGERF
     AVRNSGAKVV IEGCGSNGCE YMTGGVAVIL GRIGANFGAG MTGGMAYLYD PEGLARDYIN
     AETLVLCPVT QAHWEGELKG LIERHYQETR SRRAEEILQN WEDEKANFLQ VCPREMLPHL
     KHPIAPVEDL AAVPAE
//
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