ID U5RZ45_9CLOT Unreviewed; 1512 AA.
AC U5RZ45;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Glutamate synthase large subunit {ECO:0000313|EMBL:AGY78051.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:AGY78051.1};
GN Name=gltB {ECO:0000313|EMBL:AGY78051.1};
GN ORFNames=CAETHG_3850 {ECO:0000313|EMBL:AGY78051.1};
OS Clostridium autoethanogenum DSM 10061.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY78051.1, ECO:0000313|Proteomes:UP000017590};
RN [1] {ECO:0000313|EMBL:AGY78051.1, ECO:0000313|Proteomes:UP000017590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY78051.1};
RX PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT "Comparison of single-molecule sequencing and hybrid approaches for
RT finishing the genome of Clostridium autoethanogenum and analysis of CRISPR
RT systems in industrial relevant Clostridia.";
RL Biotechnol. Biofuels 7:40-40(2014).
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; CP006763; AGY78051.1; -; Genomic_DNA.
DR RefSeq; WP_013238397.1; NZ_CP012395.1.
DR MEROPS; C44.003; -.
DR KEGG; cah:CAETHG_3850; -.
DR PATRIC; fig|1341692.11.peg.3870; -.
DR HOGENOM; CLU_000422_8_2_9; -.
DR Proteomes; UP000017590; 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:AGY78051.1}.
FT DOMAIN 23..420
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1512 AA; 167128 MW; 0BA05F67088EE966 CRC64;
MKYNLGFPSK QGLYDPDYEK DSCGVGFIAS IKGEKTHDIV KKGVKILVNL THRGAVGADT
KTGDGAGILV QIPDEFFRIN CDNLGIELPE PGEYAVGMVF FPKETAIRLQ CEGILERAAE
EEGQKILGWR DVPTDNRSIG ETAKGTEPII RQIFIGKNAQ NQTDFERKLY IIRKKVENEV
KKTLESAAKS FYVCSLSSKT IVYKGLLLAD QIKKFYIDLN DINFKSAIAL VHQRYSTNTF
PTWDLAQPFR FLGHNGEINT IRGNRNWMRS REGVLKSEAF GKDIKKLFPI ISEGGSDSAS
LDNVLELLYE DGKSLPHALM LLIPEAWEGN KYMEEYKRAF YEYHGSLVEP WDGPAAVAFS
DGVQVGATLD RNGLRPLRYM ITKNGLVVLA SETGVLEFKD EDIEEKGKLK PGKMFLVDTA
QGRIIDDEEL KRDICKSKPY EEMLPKLKFT LDMFNAVRTR EEIPPVVLKE KQQAFGYSLE
DLSKIIGPMA RDGKEPVGSM GNDTPLAVLS NKNQLLFAYF KQLFAQVTNP PIDSIRERLV
MSLANYIGST QANILNGKDG EISNDPFIEI KSPTLTNEEI SKIKSLRDKN FKTTTIPITF
KCDTGVEGFK EALEKICERA SKRIKEGYNI LVLSDKNVDS YEAAIPSLLA VSAVQHHLIR
EKTRTKVSII VETGEARETT HFALLISYGA SAVNPYLVYQ TIDEMIKEKD IVGIKPEEAK
KNYIKAINQG ILKILSKMGI STLQSYHGAQ IFEAIGLDSE FVNKYFEGTS SRIGGIGIDV
VAKEVLARHK NAFNKIRKPI SELNVGGNYS WRKGGEFHLF NPETIYKLQV AARTNDYGMY
KQYAKVINEQ DKNLCTIRGL FQFKKGNEIP IEEVEPVSEI LKRFCTGAMS FGSISKEAHE
TIAIAMNRIG GRSNTGEGGE DPDRYVLDPN GDSRRSAIKQ VASARFGVTT EYLANADEIQ
IKIAQGAKPG EGGQLPGRKV NKYIAKIRYS TPGIDLISPP PHHDIYSIED LAQLIYDLKN
VNPSAAISVK LVSEVGVGTI AAGVAKAHAD LILISGHDGG TGASPMSSVK NAGIPWELGL
SETQQVLLLN DLRSRVRIQT DGQLKTGRDV AIAALLGAEE FGFATTALVV MGCTMLRKCH
LNTCDMGIAT QDPELRKNFK GKPEHIINFL TFIAQEVREY MAKLGFKTMN EMVGRVDMLE
TKKAITHWKA KGLDLSAILY KPYMPKRIKS YCVIPQDHGL DKAIDYKLIQ MTQKAVQDKI
KVTANLEIKN VNRSVGTMLS GTIAKKYGAK GLPEDTIVLN FKGSAGQSFG AFGINGLTLL
LEGDANDYVG KGLSGAKIVI KTPEKATFVA EKNIIAGNTI LYGATSGKVF VNGTVGERFA
VRNSGAIAVA EGVGDHCCEY MTGGRVVIIG QTGRNFAAGM SGGIAYVLDE DDSFDRKCNM
EMVEIAQMAD EDDVNTVYSL IQEHYKYTDS AKAKKILEKW DVYKTKFKRV IPTAYKLILE
QTKLEAAAAS NM
//
