ID D0LT42_HALO1 Unreviewed; 1526 AA.
AC D0LT42;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:ACY19178.1};
DE EC=1.4.7.1 {ECO:0000313|EMBL:ACY19178.1};
GN OrderedLocusNames=Hoch_6714 {ECO:0000313|EMBL:ACY19178.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY19178.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY19178.1, ECO:0000313|Proteomes:UP000001880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC {ECO:0000313|Proteomes:UP000001880};
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(2010).
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; CP001804; ACY19178.1; -; Genomic_DNA.
DR RefSeq; WP_012831770.1; NC_013440.1.
DR STRING; 502025.Hoch_6714; -.
DR MEROPS; C44.003; -.
DR KEGG; hoh:Hoch_6714; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_7; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000001880; Chromosome.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016041; F:glutamate synthase (ferredoxin) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:ACY19178.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001880}.
FT DOMAIN 28..425
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 913..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1526 AA; 167785 MW; 58A7C2D3D34323F8 CRC64;
MEDRNTESPH RPRDRWGLYE PDTEHDACGI GFVAHIRGEK SHDIVEQGLE ILRRLSHRAA
TGADPLTGDG AGILLQLPHR FFKAEGLRLG FDMPRRRRYG IGQVFLPPDR KARAACEEIL
EEVIAEQGQA VLGWRDVPTD STHIGTVARD VLPKFRQIYI RMRRVPPTAF ERKLYIIRKL
AENRVRARGV DEGGYFHVAS MSTETIVYKG LLLPGQLSNF YRDLNAPDMV SAIALVHSRF
STNTFPTWDL AQPFHYIAHN GEINTLRGNR NWMEARRSQL QSAKFGGAMD RLFPIIVPGK
SDSAQFDNML ELLHLGGRNL PNAVMMMIPE AWERHDLMDQ ERRDYYHYSS SLLEPWDGPA
AIAFTDGSIV GATLDRNGLR PARYMVTEDE RVILASEVGV IDVPPERVRM KGRLKPGRMF
IVDTGEGRIV NDEELKHDIS HRFPYRKWLS KNVFELDQVP YVEPPPPLVG AELTRLQRAF
GYTDEDLRVL LSPMAETGKE PVGSMGTDTP LAVLSERAPN LFNYFHQLFA QVTNPPIDPI
REALVMSLDS DIGPDGNTFD ETPEQCHKLR LDNPILTNAA LARVASVREG VFEAARLSLL
FDVDSGPGGL QAAVERLCQQ AEEAVDDGAS VLILSDRGVD AKRVAIPVLL ALSAVHLQLV
REGTRMQAGL VVETAEAREV HDFAVLLGYG AATVNPYLAL ESVRELAEED ILACTADEAE
ANYIAAVCGG LLKIMSKMGI STLHSYRGAQ IFEAVGLDRT LIEQYFSGTR SRLEGVGIEE
LGRELFERHD RGFGRQAVAI NDELPVGGLY QWRRRGELHK WNPATIAKLQ AAARLNDAGL
YAEYARLVDD EDQGLASLRG LMAFAEDAAT PVPLEEVEPA SDIARRFVTG AMSFGSISAE
AHETLAIAMN RLGGRSNSGE GGEEPHRFER DDNGDWRRSA IKQVASGRFG VTAHYLVNAE
DLQIKIAQGA KPGEGGQLPG HKVDERIAKV RCSTPGVTLI SPPPHHDIYS IEDLAQLIYD
LQAVNPTARV SVKLVSEVGV GTVAAGVAKG HAGCVVIAGY SGGTGASPLS SVKHAGLPWE
LGLAETQQVL VQNSLRGRVR LQVDGGFRTG RDVIIAALLG AEEFGVASAA LIVEGCIMLR
KCHLNTCSVG IATQDPELRK RFAGNPDHVV NFFLLMAEEI RGYMAKLGFR RFDDMIGRVD
MLRARPRDDH WKGKRIDLSA ILTPPRAPAS WPRRFVEPHP WDLTNHIDNR LLPQLEDAIE
RAKPVRLESA IDNTCRSAGT VLSGHIARRH GAKGLPDDTI HVYFQGSAGQ SFGAFLSSGV
TLELEGEAND YVGKGLSGGR IVVYPPRVSR FEADSNVIVG NTLLYGATAG EVYICGVAGE
RFAVRNSGAR AVVEGVGDHG CEYMTGGVVV VLGETGRNFA AGMSGGTAFV YDKDRSFRRR
CNTGMVELES LVEESEIWLV YGMVEDHVRL TGSRLGSYVL DNWENLVSHF VKVMPTDYKR
VLQARRAARR PPSATPRLAV VEGGMS
//
