ID A0A224WW90_9LACT Unreviewed; 1500 AA.
AC A0A224WW90;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Glutamine amidotransferase type-2 domain-containing protein {ECO:0000259|PROSITE:PS51278};
GN ORFNames=RsY01_187 {ECO:0000313|EMBL:GAX46608.1};
OS Lactococcus reticulitermitis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=2025039 {ECO:0000313|EMBL:GAX46608.1, ECO:0000313|Proteomes:UP000218689};
RN [1] {ECO:0000313|Proteomes:UP000218689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs-Y01 {ECO:0000313|Proteomes:UP000218689};
RA Ohkuma M., Yuki M.;
RT "Draft genome sequence of Lactococcus sp. strain Rs-Y01, isolated from the
RT gut of the lower termite Reticulitermes speratus.";
RL Submitted (AUG-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:GAX46608.1}.
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DR EMBL; BEDT01000001; GAX46608.1; -; Genomic_DNA.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000218689; 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:UP000218689}.
FT DOMAIN 21..399
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1500 AA; 164786 MW; 1FB1578F7822E7CA CRC64;
MDKLQARQQT LWDQSFESDA CGMGFIAQID GKPTHELVDY AMTILERMNH RGGTGAEPDT
GDGAGALFAM PHDFFTKIAT ENSITLPNSG DYAVGQFFLP KAADKKAALC QSISNEMQAD
GYQILMTRDV PFNFDNCGPG AQAIMPAFVQ FIVSKPSDSK SGRDFEDRLY RLRRKLEKTF
ATSEMFICSL SSKTIVYKGM LHAFQVRTFY PDLSDPAFKS TIALTHSRFS TNTFPSWDRA
QPFRFLAHNG EINTLRGAEN WMTSHKIEIY NEENSDSAKL ENCMEYLYRN GRDMPHALLM
MIPEAWGKEA GLSPELTSFY EYTSSFMAPW DGPAALVFTD GDTVGARLDR NGLRPSRYSI
TKDNFIVCSS ESGVVDFEPS RVVEKGVLGP GNMMLVDTVN GKILRNEEVK KHYAAQFPYE
KWLEHNLLHI NDLTAQAAFE DISEDDRQTM HKLFGYTEEV IRTVIVPMAE NGQEPVIAMG
YDSPLAVLSQ KNQSLFTYFK QQFAQVTNPP IDAIREKIVV GTEVYLGRDG DLRVDSDENC
VKLKLDSPVL RTEDFEKIAA LSDKKHQAQT ISTLYDVTKD TPNRLEHALV DMFKVVEAAV
DKGASIIILS DRDQKEGLMP MPILLATSGL YNYMVEKGKG SQFSIVVDTA EVNEVHHFAT
IVGYGASAIH PYGAYETLKD YNLSDKAESF RQAAEKGIIK VMSRMGISTV SGYKGAQLFE
AVGLSDAVVD KYFRGTVTRI GGLTLNQIEA EYLERYDFAY GHRSHEILPS GGSFQFKADG
EHHIFNPLTI YNFQKAVRQG DYDLYKAYSA ELDLEADETP SNLRHIWEFK GERTPVALSE
VEPVENIVKR FKVGAMSFGS LSKEAHETIA AAMNSIGAKS NSGEGGENRA RFHKQADGTN
LNSKIKQVAS GRFGVNAEYL MSAEELQIKL AQGAKPGEGG QLPGGKAFPW VAEIRGSTPG
VTLISPPPHH DIYSIEDLAQ LIYDLKAINP YAKINVKLVS STGVGTIATG CVKAGADKVV
ISGYDGGTGA SPRNSARDAG LPWEMGLAEA HQTLTMNHLR QRMTLETDGK LMTGRDVAVA
ALLGAEEYSF ASLALVAVGC VMMRVCSLNT CPVGVATQNP ELRAHFAGKP EHVVNGMKFL
AQELREIMAD LGFRSVDDMI GHAEVLKPKF IAKGKAKSLD FSRIIGTTMP IDRKVVDPFI
EERQWRELDG FAKAAIDSGT GVTVKESINN VTRTAGARMA GWIAERYGNY ELEPGLLKYE
YTGIAGQSFA SFATQGMEIT LIGEANDYIA KSLSGGRVIV KPPVDAGFNV EASPIVGNVS
LFGAVRGEAY FRGRAGERFC VRNSGAKVVV EGVGEHGCEY MTGGVAVILG STGQNFAAGM
SGGVAYVYDA KGDFADKVNM EMVDLYKVGQ TRGDDVLKEM VENHATYTAS EKAKALLADW
DNVVDKFVKV YPREFHEIKE IEYHLSRTGL AGSELEMATF EKAMRTPAAE KAELIKVGGK
//
