ID I3ZFJ8_TERRK Unreviewed; 1509 AA.
AC I3ZFJ8;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Glutamate synthase family protein {ECO:0000313|EMBL:AFL88016.1};
GN OrderedLocusNames=Terro_1714 {ECO:0000313|EMBL:AFL88016.1};
OS Terriglobus roseus (strain DSM 18391 / NRRL B-41598 / KBS 63).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=926566 {ECO:0000313|EMBL:AFL88016.1, ECO:0000313|Proteomes:UP000006056};
RN [1] {ECO:0000313|EMBL:AFL88016.1, ECO:0000313|Proteomes:UP000006056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18391 / NRRL B-41598 / KBS 63
RC {ECO:0000313|Proteomes:UP000006056};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Munk A.C.C.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "Complete genome of Terriglobus roseus DSM 18391.";
RL Submitted (JUN-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}.
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DR EMBL; CP003379; AFL88016.1; -; Genomic_DNA.
DR RefSeq; WP_014785585.1; NC_018014.1.
DR STRING; 926566.Terro_1714; -.
DR KEGG; trs:Terro_1714; -.
DR PATRIC; fig|926566.3.peg.1695; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_0; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000006056; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006056}.
FT DOMAIN 32..402
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1509 AA; 161236 MW; 3ECCFD39C4AF0455 CRC64;
MDTCFLPARP EVVSARTSVR SLVDPRFDHD SCGVGFVADS GNVASHKVLT DALTALARLA
HRGAVAADGK SSDGVGITSA VPRALLLAET GVTLDDAQPL GVGVIFVREK GANTCTVLDE
CLAEQGITVL TWRDVPVKPE VLGEIALGTM PEIRHVLVTG APEDFERKLY LARKTFERRL
EAGEVTGYVA SLSSKTMVYK SMCSGRLLPE FYPDLQNESF TTPFALFHQR YATNTTPAWH
RAQPGRTLAH NGEINTVWGN RARMEARYST LPSECQPILT QDGTDSTSLD ETVELLMHNG
RTIAEAIRVL LPPAVAGRDS AFLKYHMDTM EPWDGPAALG FTDGRYVGAA LDRNGLRPCR
FAITTDGLVV AGSEAGLVDL DPETVTHSGR LGPGQMLVVD LQEKKIYENE ELLDLFDADG
SYAALIDDTT ISAEWVDLPA TDFEAIAKSQ RNFGYTKEDV RMVLTPMATD GKDAVWSMGD
DTPLAYLAKT PRPVYAYFRQ RFAQVTNPAI DPLREAIVVS LHTRLGPWSH MLNKQASLRG
MALPSPFLSI GKLESLRQGR YPHNDTLRLR ELKCVFSSRF SLEVGIEALC TNAVELVKEG
VEILLLSDRN ADTDLLPIPM AIAVSVVHHA LVKAGLRTAT GIAVEAGDVR DVHHAAVLIG
YGAGAVCPWL ALETARATAG PDGDAKVPEI KMLKAFDAGL AKIMSKMGVS VVDSYRGAYP
FDILGLSNEV VNRCFPNTPA PLGGVGFAEI EHGIRQLWGA PVSPDLQAKI DLPDYGWVKF
RKADMAEPHA WQPSNVKALQ SVVGSARNVP MPEDAAKAFQ IYSTAVATKE TPTVLRELLE
IRPAGPELDL DKVESPRSMM KRFAASAMSL GSLSPEAHTT ITIAMNSIGG KSNTGEGGED
SDVYRPHPGN RRVLMPGEAS AFVNKPSPGG VAVAEPIVEA PAVHSFLNNK IKQVASGRFG
VTAEYLAHAE EIEIKVAQGA KPGEGGQLPG HKVTGLIARL RHAQPGVPLI SPPPHHDIYS
IEDLAELIHD LKRVNPRAAV GVKLVSSCGV GTVAAGVAKA YADYVVIAGN VGGTGAAALS
SIKYAGNPWE LGLAEAHQTL MANGMRGRVR LRTDGGLSTA RDVLIAAMLG ADEFAFGTAV
LVVLGCDMAR QCHLNTCPTG IATQKPELRA RFRGKPEHVV RFFEQLSGDL QQMLARYGLA
SIEEAIGRVD LLEQVRFDGG LDLSPMLVQE GNGPRKWDGI RNDRPETEPA LDDAWVAPAV
AAFEKGEAYS VSGMIANKDR AVGARIAGEM TILQAKAESP MPLPDVTIKL TGTAGQSFGA
FAIEGMKLEL TGEANDFVGK GLSGGEIVIR ARGLAKTKSG AHVLLGNVAL YGATAGKLFV
AGQAGERFAV RNSGATAVVA AVGDHGCEYM TGGTVVVLGS IGLNFGAGMT GGIAWLYDAE
GTVLSGSRYH ADFLQAIPFA ETDEAAQAEL KSLLEEHGAK SESTRAARFL SDWDTHSKKF
LRMVPISQV
//
