ID D8EZP3_9DELT Unreviewed; 1529 AA.
AC D8EZP3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Class II glutamine amidotransferase {ECO:0000313|EMBL:EFK10962.1};
GN ORFNames=NPH_4970 {ECO:0000313|EMBL:EFK10962.1};
OS delta proteobacterium NaphS2.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=88274 {ECO:0000313|EMBL:EFK10962.1, ECO:0000313|Proteomes:UP000003834};
RN [1] {ECO:0000313|EMBL:EFK10962.1, ECO:0000313|Proteomes:UP000003834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NaphS2 {ECO:0000313|EMBL:EFK10962.1,
RC ECO:0000313|Proteomes:UP000003834};
RX PubMed=21124915; DOI=10.1371/journal.pone.0014072;
RA Didonato R.J., Young N.D., Butler J.E., Chin K.J., Hixson K.K., Mouser P.,
RA Lipton M.S., Deboy R., Methe B.A.;
RT "Genome Sequence of the Deltaproteobacterial Strain NaphS2 and Analysis of
RT Differential Gene Expression during Anaerobic Growth on Naphthalene.";
RL PLoS ONE 5:E14072-E14072(2010).
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:EFK10962.1}.
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DR EMBL; ADZZ01000144; EFK10962.1; -; Genomic_DNA.
DR Proteomes; UP000003834; 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:0016740; F:transferase activity; 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 ECO:0000313|EMBL:EFK10962.1}; 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:UP000003834};
KW Transferase {ECO:0000313|EMBL:EFK10962.1}.
FT DOMAIN 35..435
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1529 AA; 167317 MW; 8E3D6267FA01434D CRC64;
MKPQKEMVMS QYENRFGAYP PSQGLYRGRY EHDSCGVGFV ANIDGHKDHD VIVNGLKVLE
NLMHRGAIGG DQTTGDGAGI LFQLPELFFK KVCTKQNIVL PPVGRYGVGM VFLPMDSGLG
NGWVREIEQA VSGEGLTFLG WRDVPVNEGV IAGQARATQP LIRQFFVDGG SLEGAALERK
LYVTRKVIEK RFMALEASGG ESAGKCYLPS LSCRTIVYKG LFTAQQLVGF YEDLKDPEMV
SVLAVVHQRY STNTFPSWEL AQPFRYMAHN GEINTLRGNL NLVRAREQAL SSPLFGKEME
KLLPIIDERG SDSACLDNAL ELLTSAGRSL SHAMLMLIPE AWGVKYPMGP DQRGFFEYHA
GLMEPWDGPA AVSFSDGSQV GAMLDRNGLR PARYTITRQG MVVFASEAGV LEIAPEDVLE
KGALGPGRMI LVDFEKKRVL KNGEIKNLNA RRQPYRRWVE ENRVSLRGFY GEVASIKPDF
ARLPFHQKLF GYTREDLQMI IGPMATGGQE PVGAMGADTP LAVFSEKNQL LFGYFKQLFA
QVTNPPIDPV REELVMSLMT FIGNPGNILA ETPRNSRLIK LLHPIITNED LIRLTDLNVE
GFRAEIVKIG FPVEGGGVML EAALDRISKE SESAISKGHQ LIILSDRDLP EGTAPIPSLL
AVSAVNQHLI GEGIRTSAGL IVETGEAREV MHMALLLGYG ATAVNPYLAF ETVAAMSVRK
ALGREMGTAV SIEKYIKALC KGLLKIMSKM GISTLRSYRS AQVFEAVGLN TKVVDRYFRG
TDSRVEGIGL DEIAKEAVDR YHFACHPAPD VPSILPSGGH FNVRVDGERH LWTPEAIHHL
QRAVRENDAA FYARYAEAIN DQSEKQSTLR GLFAFRKTDP IPLEEVEPAS EIVKRFFTGA
MSFGSISREA HETIAIAMNR LGGCSNSGEG GEDPARYVPL ENGDSRSSAV KQVASGRFGV
TAEYLVNAKE IQIKIAQGAK PGEGGQLPGH KVNLEIARVR YSTPGVTLIS PPPHHDIYSI
EDLSQLIFDL KNVNPEARIS VKLVSEVGVG TIAAGVSKAH ADMVLISGYD GGTGASPLSS
IRHAGAPWEL GVSDTQQTLI LNGLRSRIRV QADGQMKTGR DVVVAALLGA EEYGFATAAL
VVLGCVMVRK CNNNRCPVGI ATQDEALRKR FSGKPEHLQI FFTMLAEEVR GYMAQLGFRK
MDHMIGRSDL LEMSRAIHFW KAKGLDFSKI FYFPGVDNGS PRRCIESQEH PISDVLDKDL
ITQARKALDH GERVEISSPI RNINRTAGAM LSGEVAKRYG NQGLPADTIL CRFQGAAGQS
FGAFGAKGVT FILEGEANDY LGKGLSGAKI IVKPYKDATF VPSRNVIAGN VILYGATSGE
MYLHGKAGER FAIRNSGALA VVEGVGDHGC EYMTGGRVVV LGETGVNFAA GMSGGIAYVY
DPNRRFDLRC NLDMVDLELV VTEEDEAELK NMLFQHVAHT GSPKAQSILD NWESSLPFFV
KVFPMEYRRV LGQMSKEDEE TEREEVQHG
//
