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Database: UniProt
Entry: R6D9F1_9BACE
LinkDB: R6D9F1_9BACE
Original site: R6D9F1_9BACE 
ID   R6D9F1_9BACE            Unreviewed;      1530 AA.
AC   R6D9F1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Glutamine amidotransferase type-2 domain-containing protein {ECO:0000259|PROSITE:PS51278};
GN   ORFNames=BN772_02807 {ECO:0000313|EMBL:CDA84375.1};
OS   Bacteroides sp. CAG:754.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1262750 {ECO:0000313|EMBL:CDA84375.1, ECO:0000313|Proteomes:UP000017906};
RN   [1] {ECO:0000313|EMBL:CDA84375.1, ECO:0000313|Proteomes:UP000017906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:754 {ECO:0000313|Proteomes:UP000017906};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDA84375.1}.
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DR   EMBL; CBCP010000150; CDA84375.1; -; Genomic_DNA.
DR   Proteomes; UP000017906; 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:UP000017906}.
FT   DOMAIN          35..426
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   1530 AA;  169244 MW;  00BBFDB9E9AAA4FD CRC64;
     MKKQELFNNE TKGFPYQRQP RQAGLYDAAY EHDACGVGML VNIHGEKSHD VVESALKVLE
     NMRHRGAEGA DNKTGDGAGI LLQIPHEFIL LQGIPVPEKG RYGTGLLFLP KNDKDQGAIL
     SIIIEEIEKE GLTLMHLRNV PTCPEILGEA ALANEPDIKQ VFITGFTETE TADRKLYLIR
     KRIENKVRLS SIPAKDDFYV VSLSTKSIIY KGMLSSLQLR NYYPDLTNSY FTSGLALVHS
     RFSTNTFPTW GLAQPFRLLA HNGEINTIRG NRGWMEARES VLSSPTLGDI KEIRPIIQPG
     MSDSASLDNV LEFLVMSGLS LPHAMAMLVP ESFNEKNPIS EELKAFYEYH SILMEPWDGP
     AALLFSDGRF AGGMLDRNGL RPARYLITKN DMMVVASEVG VMDFEPGDIR EKGRLQPGKI
     LLVDTEKGEI YYDGELKRQL AEAKPYRTWL STNRIELDEL KSGRKVPHHI ENYDRMLRTF
     GYSKEDIERL IMPMASTGAE PIQSMGNDTP LAVLSDKPQL LYNYFRQQFA QVTNPPIDPL
     REELVMSLTE YIGAVGMNIL TPSESHCKMV RLNHPILSNT QLDILCNIRY KGFKTVKLPM
     LFEVEKGKAG LQEALGSLCK MAEESVTEGV NYIILSDRDV DAGHAVIPSL LAVSAVHHHL
     ISVGKRVQTA LVVESGEIRE VMHAALLLGF GASALNPYMA FAVLDKLVKD RDIQLDYATA
     EKNYMKSICK GLFKIMSKMG ISTIRSYRGA KIFEAVGLSE ELSKAYFGGL GSPIGGIRLE
     EIARDAIAFH EEGFAKEVDG LLPNKGLYAF RKDGEKHAWN PETISTLQLA TRLGSYKKFK
     EYTHLVDEKE KPIFLRDFLG FRRNPISIDR VEPVENILHR FVTGAMSFGS ISKEAHEAMA
     IAMNKIHGRS NTGEGGEDAS RFQPLPDGSS LRSAIKQVAS GRFGVTAEYL VNADEIQIKI
     AQGAKPGEGG QLPGFKVNDV IAKTRHSIPG ISLISPPPHH DIYSIEDLAQ LIFDLKNVNP
     QAKISVKLVA ESGVGTIAAG VAKAKADLIV ISGAEGGTGA SPASSIRYAG ISPELGLSET
     QQTLVLNGLR GQVVLQVDGQ LKTGRDIILM ALMGAEEYGF ATSALIVLGC VMMRKCHQNT
     CPVGVATQDE ELRKRFHGRS EYLVNFFTFL AQEVREHLAE MGFTRMDDII GRTDLIERKS
     VELKSVEHMS VEYKSEAHIP NPKHTLIDFT KMLARIDNSA AIRHVIDQDH GISTVKDVAI
     IDAARDAIEH EKEISLEYTI ANTDRAIGAM LSGVIAKKQG ARGLPEHTLN VKFKGSAGQS
     FGAFLVPGVN FKLEGEANDY LGKGLSGGRI AVLPPIRSNF EADKNTIAGN TLLYGATSGE
     VYINGRVGER FAVRNSGAVA VVEGVGDHCC EYMTGGRVVV LGQTGRNFAA GMSGGVAYVW
     NKDGNFDYFC NMEMVELSLI EEAGYRKELH ELIRQHYLYT GSKLARTMLD DWNHYVDQFI
     QVVPIEYKKV LQEEQMRKLQ QKIADMQRDY
//
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