ID R9KLA5_9FIRM Unreviewed; 1513 AA.
AC R9KLA5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:EOS47011.1};
GN ORFNames=C810_01847 {ECO:0000313|EMBL:EOS47011.1};
OS Lachnospiraceae bacterium A2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=397290 {ECO:0000313|EMBL:EOS47011.1, ECO:0000313|Proteomes:UP000014150};
RN [1] {ECO:0000313|EMBL:EOS47011.1, ECO:0000313|Proteomes:UP000014150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2 {ECO:0000313|EMBL:EOS47011.1,
RC ECO:0000313|Proteomes:UP000014150};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium A2.";
RL Submitted (APR-2013) 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:EOS47011.1}.
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DR EMBL; ASSX01000008; EOS47011.1; -; Genomic_DNA.
DR STRING; 397290.C810_01847; -.
DR PATRIC; fig|397290.3.peg.2021; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_9; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000014150; 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:UP000014150}.
FT DOMAIN 21..412
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 897..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1513 AA; 167198 MW; C29BE110FCFBB0CC CRC64;
MQETKRTAMG MYDPGFEHDN CGIGAVVNIK GKKTHKTVED ALKIVENLKH RAGKDAEGKT
GDGVGILLQI SHKFFEKAAK KAGIGIGGER DYGVGMFFFS QDELKRNQAK KMFEVIVNKE
GMEFLGWREV PIVPGQLGQK AVDCMPCIMQ GFVGRPKGTE KGLEFDRKLY VARRVFEQSS
DDTYVVSLSS RTIVYKGMFL VEQLRQFFPD LQDEGYESAI ATVHSRFSTN TNPSWERAHP
NRLIVHNGEI NTIRGNVDKM LAREETMESE YLKGELQKVL PVVNAEGSDS AMLDNTLEFL
VMSGMDLPLA VMITIPEPWA NNGLMSQKKK DFYQYYATMM EPWDGPASIV FSDGDILGAV
LDRNGLRPSR YYITDDDNLV LSSEVGVLEI DPTKIVAKER LRPGKMLLVD TVQGRVIDDD
ELKEKYAGRR PYGEWLDRNL IKLADLKIPN QRVPEYRREE RQRMQKTFGY TYESLKEAIL
PMAKNGVEGT SAMGIDTPLA ALAQDHQPLF NYFKQKFAQV TNPPIDSIRE EVVTSTTVYI
GEDGNLLEEK PINCQVLKVN NPILTNTDLM KIKAMEAEGF KVVEIPIIYY KNTSLEKAID
RLFVEADRAY RDGANILILS DRGVDENHVP IPSLLAVSAL QQHLIKTKKR TALAMILESG
EPREVHHFAT LLGYGACAIN PYLAQDTVKQ LIDEHMLDKD YYAAVADYNH AILHGIVKIA
AKMGISTIQS YQGAKIFEAI GISPEVIEKY FTGTVSRIGG ITLKDIEKDV DALHSSAYDP
LGLETDLTLE SRGRHKMRSG ADSHLYNPLT IHLLQESTKR GDYQLFKEYT KAADAEEQKA
NLRGMMDFIY PKKPIPLEEV ESVDSIVTRF KTGAMSYGSI SQEAHETLAI AMNRLRGKSN
SGEGGESPER LAAGADGKNR CSAIKQVASG RFGVTSRYLV SAKEIQIKMA QGAKPGEGGH
LPGQKVYPWI ARTRLSTPGV SLISPPPHHD IYSIEDLEQL IYDLKNSNKD ARITVKLVSE
AGVGTVAAGV AKAGAQVVLV SGYDGGTGAA PSSSIHNAGL PWELGLSETH QTLILNGLRN
KVRIETDGKL MTGRDVAIAA MLGAEEFGFA TAPLVTMGCV MMRVCNLDTC PAGIATQNPE
LRKRFAGKPE YVMNFMRFIA EELREYMAKL GIPTVDGLVG RSDLLKVREG LSGREQELDL
SRILNNPFAG PKANVIFDPK QVYDFELEKT KDEQVLMKQL KFALEGGQKR SIDVEVSNTD
RSFGTIFGSE ITKRFDGALD EDTFLVKCTG AGGQSFGAFI PKGLTLELVG DSNDYFGKGL
SGGKLVVYPP AGVKYRQEEN IIIGNVALYG ATSGKAFING VAGERFCVRN SGANAVVEGV
GDHGCEYMTG GRVVVLGKTG KNFAAGMSGG IAYVLDEDND LYTRINKEMV FSEEITSKYD
VMELKDMVQE HVALTNSRKG KEVLGHFSEY LPKFKKIIPY DYNRMMTAMV QMEEKGLSSE
QAQIEAFYAS IGH
//
