ID   C7QCB2_CATAD            Unreviewed;      1550 AA.
AC   C7QCB2;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:ACU74560.1};
DE            EC=1.4.7.1 {ECO:0000313|EMBL:ACU74560.1};
GN   OrderedLocusNames=Caci_5702 {ECO:0000313|EMBL:ACU74560.1};
OS   Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS   B-24433 / ID139908).
OC   Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC   Catenulisporaceae; Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU74560.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU74560.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647; DOI=10.4056/sigs.17259;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA   Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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; CP001700; ACU74560.1; -; Genomic_DNA.
DR   RefSeq; WP_015794289.1; NC_013131.1.
DR   STRING; 479433.Caci_5702; -.
DR   KEGG; cai:Caci_5702; -.
DR   eggNOG; COG0067; Bacteria.
DR   eggNOG; COG0069; Bacteria.
DR   eggNOG; COG0070; Bacteria.
DR   HOGENOM; CLU_000422_8_2_11; -.
DR   InParanoid; C7QCB2; -.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000000851; 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:ACU74560.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT   DOMAIN          54..445
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   REGION          941..961
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        947..961
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1550 AA;  166634 MW;  39956A9B4CBB101C CRC64;
     MAFPAIPPGR PGSSRPEAQA AAQAAAASTS AAPLFSALPE AQGLYDPRAE KDSCGVAFVA
     TLTGIASHGI VDQALQALVN MEHRGASGAE PSTGDGAGIL VQVPDAFLRA VLSESGARFD
     LPPAGHYAVG VAFLPTDDDA AREAEIRVEA IAAEEHLAVL GWRELPTNPE GLGNGALSVM
     PRFRQLFVTG TGGQSGIELD RLAFALRKRA ERDAQVYFPS LSARTLVYKG MLTTAQLETF
     FPDLLDERFA SAIGLVHSRF STNTFPAWPL AHPYRFVAHN GEINTVIGNR NWMRARESDL
     ATDLIGGDLD RLFPICTPGA SDSASFDEAL ELLHLGGRSL PHAVLMMIPE AWENHGEMDA
     ARRAFYAYHS SFMEPWDGPA DMVFSDGTLI GAVLDRNGLR PSRYWVTDDG LVVLASEFGV
     LDIDPATVVR KGRLQPGRMF LVDTAAGRIV EDEEIKAALA AAEPYAEWLH AGRIKLDKLP
     EREHIVHTRA SVTRRQQTFG YTEEELRVLL APMARTGGEP LGSMGSDTPI AVLSEKPRLV
     FEYFSQLFAQ VTNPPLDAIR EELVTSLATT IGPETNLLDP TAAACRQVEV AFPVIDNDEL
     AKLIHINADG DLPGLRAVTV SGLYRVAGGG PALRARLEEI REEVSKAIAG GARIIVLSDR
     HSDAEHAPIP SLLLTSAVHH HLIREKTRTH VGLVIEAGDV REVHHVALLI GYGAAVVNPY
     LAMESVEEMA GSGHLGLIEP DQAIRNLIKA LGKGVLKVMS KMGISTVASY RGAQIFEAVG
     LAQDVVDEYF TGTTSKLGGV GLETLAEETA RRHARAYPKQ SGTSRLAHRR LEIGGEYQWR
     REGEPHLFDP DTVFRLQHST REKRYDIFKQ YTSRVDEQSE RLMTLRGLFK FKDGARAPIP
     IEEVEPISDI VKRFSTGAMS YGSISAEAHQ TLAIAMNQLG AKSNTGEGGE DVDRLRDPER
     RSSIKQVASG RFGVTAEYLA EADDIQIKMA QGAKPGEGGQ LPGHKVYPWV AKTRHSTPGV
     GLISPPPHHD IYSIEDLAQL IHDLKNANRD ARVHVKLVAE VGVGTVAAGV SKAHADVVLI
     SGHDGGTGAS PLTSLKHAGA PWELGLAETQ QTLLLNGLRD RIVVQTDGQL KTGRDVLIAA
     LLGAEEYGFA TAPLVVSGCV MMRVCHLDTC PVGVATQNPE LRARFNGRPE FVVTFFEYLA
     EEVREHLAAL GFRSLQEAVG HAELLDTSAA VAHWKASGLD LAPLLHVPAL PEGTALHRTR
     EQDHGLDKAL DHQLIAVAQP AIARREPVRA QFQIRNVNRT VGTMLSHEVV KAHRGEGLAE
     GTIDLTFVGS AGNSFGAFLA PGITLRLEGD ANDYVGKGLS GGRIVVRPHR EAATINDAAE
     RNVIAGNVIA YGATSGRIHL RGTVGERFCV RNSGATAVVE GVGDHACEYM TGGTVVVLGE
     HGRNLAAGMS GGTAYVLDLK VSRVNSEMVN VEALDAEDRA LLHTLVQEHQ EETGSAVAEA
     LLADWGAHVG RFAKIMPVDY KRVLTARAAA QAAGLSEEQT LDKIMEATRG
//