ID Y0KKM3_9PROT Unreviewed; 1554 AA.
AC Y0KKM3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Glutamate synthase family protein {ECO:0000313|EMBL:EUJ11767.1};
GN ORFNames=Meth11DRAFT_2614 {ECO:0000313|EMBL:EUJ11767.1};
OS Methylophilaceae bacterium 11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae.
OX NCBI_TaxID=1101195 {ECO:0000313|EMBL:EUJ11767.1, ECO:0000313|Proteomes:UP000022668};
RN [1] {ECO:0000313|EMBL:EUJ11767.1, ECO:0000313|Proteomes:UP000022668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11 {ECO:0000313|EMBL:EUJ11767.1,
RC ECO:0000313|Proteomes:UP000022668};
RG DOE Joint Genome Institute;
RA Chistoserdova L., Huntemann M., Han J., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Palaniappan K., Ivanova N., Schaumberg A.,
RA Pati A., Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JUL-2013) 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:EUJ11767.1}.
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DR EMBL; JCKJ01000001; EUJ11767.1; -; Genomic_DNA.
DR STRING; 1101195.Meth11DRAFT_2614; -.
DR PATRIC; fig|1101195.3.peg.2561; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR Proteomes; UP000022668; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000022668}.
FT DOMAIN 40..437
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1554 AA; 168740 MW; 8761202B63D8E50B CRC64;
MQAVNTPETL EQTQATMQAH TGLAPKSQGL YDRRNEKDSC GVGFVAHIKG KKSHDIVAKG
LELLTNLTHR GATGYDPKLG DGAGLLMQMP DAFMRKEAAK LSIELPEVGQ YAVGNLFLPQ
DQKNRAQCEA IIAKIIAEEN QTLLGWRDVP VDNGNIADAA REVEPCMRQV IVASAAKDNN
VFERKCFVIR KRIEHAVRAL NLQDKAQFYV PSFSSRTIVY KGMLLANEVG VYYKDLVDET
VVSALALVHQ RFSTNTFPAW DLAHPFRMIA HNGEINTVQG NVNWMAARHE TMKSTVIGED
LDKLWPLIAD GQSDSACFDN CLELLVAGGY SLPHAMMMLI PEAWNNNALM DEDRRAFYEY
HAALMEPWDG PAAVAFTDGK MIGATLDRNG LRPARYLVTE DDIVMMASEM GVITFPQEKI
IKKWRLQPGK MLLIDMEQGR IIDDNEAKKQ LANAKPYRQW IEQSRYHLSD LPKIEVNLTL
NETLLDTQQA FGFTQEDIKF VLQPMVANGE EGAGSMGNDA ALPVLSNKPK QIYNYFKQLF
AQVTNPPIDP IREELVMSLV TFIGPKPNLL SVDETNPPLR LEASQPVLML EELEQLKNIE
SSTKGQYKSL VLDITYDAAL GKAGMANAIK ALHEQAVKAV HAGINVLILS DRAIAKNRVA
IPALLACSAT HEHLVKEGLR TSTGLVIDTG SAREVHHFAL LAGYGAEAVC PWLTFETIKH
LSDDAYKAQK NFVKAIGKGL YKVMSKMGIS TYQSYCGAQI FEAIGLNTAF VNEYFTGTAT
QIEGIGIEQV AEEALRLHNS AFGNDPVLAN ALDAGGEYAF RVRGEEHMWT PESISKLQNA
TRTGKYDTYK EYAKLINDQT RRHMTLRGLF EIKPLGTAIP LEQVESAKEI VKRFATGAMS
LGSISTEAHA TLAIAMNRIG GKSNTGEGGE DAKRFIPVAN ATTMAQVIGE DLVESNIPLK
AGDSMRSRIK QVASGRFGVT ANYLASADQI QIKMAQGAKP GEGGQLPGHK VSPYIAQLRF
SVPGVGLISP PPHHDIYSIE DLAQLIHDLK NANPKASISV KLVSETGIGT VAAGVAKAKS
DHIVVAGHDG GTGASPISSI KHAGTPWELG LAETQQTLVL NQLRGRVVVQ VDGQMKTGRD
VLIGALLGAD EFGFATAPLV VEGCIMMRKC HLNTCPVGVA TQDPELRKKF TGQPEHVVNY
FFFVAEELRE LMASMGVAKF DDLIGRADLL DMKAGIEHWK INGLDFSKVF HLPAMPASVS
RKNNDVQDHG LVNALDNKLI ALAKPALEKG EQVNIDIAIT NTNRTVGTML SNQIASRYGA
QGLPNGTIHV KFTGTSGQSF AAFLAKGITF ELTGEGNDYV GKGLCGGRII IKPPVTFRGI
SHENIIVGNT VMYGATTGES YLSGVAGERF CVRNSGASAV VEGVGNHGCE YMTGGTVVVL
GLTGQNFAAG MSGGVAYVYD EDGMFAQRCN MSMVTLEKVE AADADVGKVQ HLGQPDEVTL
KSLIENHAQL TGSTRAKALL ADWTNARTKF VKVMPNEYKR ALTELAAATA KQAA
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