ID D5EKD8_CORAD Unreviewed; 1551 AA.
AC D5EKD8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE SubName: Full=Glutamate synthase (Ferredoxin) {ECO:0000313|EMBL:ADE54887.1};
DE EC=1.4.7.1 {ECO:0000313|EMBL:ADE54887.1};
GN OrderedLocusNames=Caka_1869 {ECO:0000313|EMBL:ADE54887.1};
OS Coraliomargarita akajimensis (strain DSM 45221 / IAM 15411 / JCM 23193 /
OS KCTC 12865 / 04OKA010-24).
OC Bacteria; Verrucomicrobiota; Opitutae; Puniceicoccales;
OC Coraliomargaritaceae; Coraliomargarita.
OX NCBI_TaxID=583355 {ECO:0000313|EMBL:ADE54887.1, ECO:0000313|Proteomes:UP000000925};
RN [1] {ECO:0000313|EMBL:ADE54887.1, ECO:0000313|Proteomes:UP000000925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45221 / IAM 15411 / JCM 23193 / KCTC 12865
RC {ECO:0000313|Proteomes:UP000000925};
RX PubMed=21304713; DOI=10.4056/sigs.952166;
RA Mavromatis K., Abt B., Brambilla E., Lapidus A., Copeland A., Deshpande S.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Han C., Detter J.C., Woyke T.,
RA Goodwin L., Pitluck S., Held B., Brettin T., Tapia R., Ivanova N.,
RA Mikhailova N., Pati A., Liolios K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Coraliomargarita akajimensis type strain
RT (04OKA010-24).";
RL Stand. Genomic Sci. 2:290-299(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; CP001998; ADE54887.1; -; Genomic_DNA.
DR RefSeq; WP_013043609.1; NC_014008.1.
DR STRING; 583355.Caka_1869; -.
DR MEROPS; C44.003; -.
DR KEGG; caa:Caka_1869; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_0; -.
DR OMA; TVFRLQH; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000000925; 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; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
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:ADE54887.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000925}.
FT DOMAIN 23..424
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 933..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1551 AA; 169947 MW; A4E82D14FBB529C8 CRC64;
MEHTYTQPKA QGLYDPQNEH ENCGIGLIVD MKGRKSHDIV QGALEICVNL DHRGGCGCDP
ITGDGAGIFI QLPHNFFKAV CKEEAGFDVP EDGDYGVGFV FLSQDQEERT NEENIIGEII
AEEGFELLGW RDVPVKSEIL GKASKACEPV MRQFFIARGD VCERGLAFER KLYLIRRTAT
HRIRYSGQDE ESLFYISSLS SRTMTYKGML TTEQLGDYFP DLAHEAMDSA LALTHSRFST
NTFPSWPRAQ PFRYLCHNGE INTVRGNENW LHARQMQLAS EVFGDDLQKL LPIIREDGSD
SQKFDNCLEF LVLSGRSLAH AMMMMIPEPW ERHKSMPQFK RDFYEFHACM MEPWDGPASM
AMSDGVQVGA TLDRNGLRPS RYYVTADDRV ILASEVGVLE GIEPKNVVKK GRLEPGRMFL
IDMEEGRIVD DAELKEQIAA ENPYGEWLKD NLVPADTLPA PEADQTPADN FETLETRQKA
FGYTFEDMRF IVGPSAQTGK QPLGSMGNDA PLAVLSDQPQ LMYNYFKQLF AQVTNPPIDP
IREELVTASV TFIGSEGDLT RPGPESCRMI KFETPLLSDA ELAQLRYINK DGFKATKLPI
TFEAEVGGMA TGHNSVPEPS ISGKGLEGAL EKLFENADAA IRDGVNILIL SDRKVGPNKA
PIPALLAVAG LHHHLVRQGT RTRVSIVLES GEPREVQHFA LLLGYGANAI NPYLALETVR
HLVDRGDLDV DPDKACANFL KANLGGVIKT MSKMGISTVA SYRGAQIFEA IGLNQAVIDK
YFTKTASRVE GIGLGTIAKE TESRHQKAFA PRDDERDAAL DTGGIYQWRA NGERHLFNPV
TIHKLQMATR FGDYAVFKEY SDAINDQSKE MFTLRGLMDF KIDESKSIPI EEVEPIEEIM
KRFKTGAMSY GSISKEAHEA IAIAMNRIGG KSNTGEGGED IDRFTPDENG DSRRSAIKQV
ASGRFGVTSY YLVNSDEIQI KIVQGAKPGE GGELPGHKVL PQIAKTRGTT PGVGLISPPP
HHDIYSIEDL AELIHDLKNS NVNARVNVKL VSEVGVGTIA AGVAKAKADV ILVSGYDGGT
GASPRSSIQH AGAPWELGLA ETNQTLLLND LRSRVVVETD GQLKTGRDVA IACLLGAEEF
GFATTALVTL GCLMMRVCHK NTCPVGVATQ NPELRKKFNG DAESVVNFMK YIATEVREYM
AKLGYRSINE MVGQVQNLEM RKAVDHWKAK GLDYSKILYK PEVGPEVGTF CQMKQDHLLD
KCLDMREILE QAQPAVKDGK AVEINLPIIN TDRVVGTITG AEISRNHGPD GLPEDTVQIN
LTGSAGQSLG AFCPQGMTFT VTGDTNDYLG KGLSGGKIVV RPSEDSPFVA HENIITGNVC
FYGATKGEAY IAGMAGERFC VRNSGVEAVI EGVGDHALEY MTGGMVINLG TTGRNLGAGM
SGGVAYVFDE AGDFVQHSLN PDMVNVYQLI ECGDDEINLV KAKIEKHVEL TGSKRGQAIL
ADWPAIAGKF LKIMPQDYER VLQAQARAEE RGLKGDDAIL AAFEENVKAG H
//