ID A0A0F6A7N9_9GAMM Unreviewed; 1809 AA.
AC A0A0F6A7N9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Glutamine amidotransferase type-2 domain-containing protein {ECO:0000259|PROSITE:PS51278};
GN ORFNames=N479_18615 {ECO:0000313|EMBL:KKE82252.1};
OS Pseudoalteromonas luteoviolacea S4054.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1129367 {ECO:0000313|EMBL:KKE82252.1, ECO:0000313|Proteomes:UP000033434};
RN [1] {ECO:0000313|EMBL:KKE82252.1, ECO:0000313|Proteomes:UP000033434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4054 {ECO:0000313|EMBL:KKE82252.1,
RC ECO:0000313|Proteomes:UP000033434};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KKE82252.1}.
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DR EMBL; AUXW01000166; KKE82252.1; -; Genomic_DNA.
DR RefSeq; WP_046357242.1; NZ_AUXW01000166.1.
DR PATRIC; fig|1129367.4.peg.3777; -.
DR Proteomes; UP000033434; 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; 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}.
FT DOMAIN 15..398
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1809 AA; 198318 MW; 61F738E18E72DC1E CRC64;
MKRYLFDKDL DKSSCGVGFI THKQSLKTHQ LIQHAHQALC MIPHRGGMNA EGIGDGAGVN
IDLSLTFFRK VTQHSNLELG EFGVANFFLP NDIANREEAI SLINRVLTEH KLEVITTRDV
ETDSSVLNPD SQKAQLVIKQ FVFTRPVHIS SQSVFESLIH QALEDIELHA FTTESLRGLY
PLSMSSQTQV LKGRLNSWEV IPYFKDLSDP EQQVHTLFFH TRFSTNTAPN PMFAQPFRRM
AHNGELNTDR KNRLSENAIA KYKNKRLIFP AGQSDSARLD QTLARRVIED DMPIDVAALA
MMPPAWENDE SLSKPVRAML EYFSLYEEKN DGPAAFIFGD GVKVGARLDR LGLRPLRSVE
THDYLAVMSE AGQIDFPEEE IVRRGRIEAG GMIVFDHQHK EIKLTAQILE ELAAEHDYTA
LLDKARLTLE EIPAVECSDL TQNAQLNIAA QHVAYSMNQE SFKFMLDPML QDGSEKISAM
GYGLAPNVLT REEGGVSRYF SQRFAQVTNP PLDSIREVDG MTLRVALGAK PNISPTSHRQ
IVLNSPLLKP QDLAKITTQT ALKVSTLPML FNVDPEHIDH QQQLLDALKT LACRAEQLAQ
DGCDIIILSD QAVTHQQAAI PALLAVATIN QKLIAEGLRF NTSLVCHTGQ AASTHDLACL
LGFGASAVCP ITVYNRAVEL FENEQAVLDA LARYQKAAEK ALMKTMGKFG LCTVESYIGG
EFFEANFIDT HDPLLKVIFP NIHSPVGGAR FKDLVESAVS WHKKVFEVQA EDQIPVLGLF
KERAQGAGHS FGTTAVREYI NMTEEKIQYI DESQLESTDT GVILPDDDGY KDLGFEARTP
EQIAQFKITQ AYREFSHNLL IERHHRPAAL RDVLALPLDF TQLNNTQAFI DALKLIEISG
SFQVHVRGLN VEPIAQHKWL LSHSANNTDT NHCLAEALNQ LFKTEVYEVL PANDKILIET
RTNSTLDKLC SKLISGADQI SLTDVQPAHE ITATFASGAM SHGALVEKAH EAVAQGTNIA
GAMSNSGEGG ENSRRYNTVK ASKIKQFASG RFGVWTGYLA DPALQEIEIK IGQGAKPGEG
GQLPAPKVNV VIAAARGGTP GVELVSPPPH HDTYSIEDLG QLIHDAKAAR VRVIVKLVSS
EGIGTIAVGV AKAGADVINV AGNTGGTGAA QVTSLKHTGR AADIGIAEVH QALAENGLRD
KITLRCSNAH QTGSDVVKSA MLGGDSFEFG TTALMMLKCV MAKNCNLKCP AGLTTNPEVY
RGDPRALAQY FMNVAHEVRE ILASIGYRSL AEIRGRSDLL HLVSHPAMVG KLDMTAMLKP
AQEIKITTPI YLEANFDIDS TWLQQLESHF LATKLTQFES EPVKLNNCNK TVGGQLAIDI
ERILNYRLSD TDIENHPAIM CLENGRKTLK PNSIKLHTTG SAGQSYGAFN NSGMLLRHIG
TCNDGVGKGA SGGQIIVSSG QNSIEENVLI GNFALFGATG GQLYVNGQAG DRFGVRNSGA
VAVIEGVGDF CCEYMTNGAI VNIGAYGKGF GNGMSGGTAY QYDPSGRISE LCSQDSVTAL
QLGEDNALCK GQEQALLQHL TDHVTATSSL KVKALLDGWQ TAKQHFYVLI PNALFQYHCA
DRIVQTLNRR AMLEELSQGW ADQSVKTIKH AYQDYHNTNV SLFDGELPAY GDCDTDLVYR
YISSAGILHR ADQLVQKQHA QGYTEVSAHY LFDTLDHKLI DALAKDAKEA LASYDDQALS
CLLAQKRVQD YKEALSLREV CDSPAIGTSV WIIHRDKAVQ QALREYRCLN ELLATHYCHV
LSEAVRYAA
//
