ID A0A1Q6ZU05_9CHLR Unreviewed; 1513 AA.
AC A0A1Q6ZU05;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:OLB53330.1};
GN ORFNames=AUI01_11980 {ECO:0000313|EMBL:OLB53330.1};
OS Ktedonobacter sp. 13_2_20CM_2_56_8.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805232 {ECO:0000313|EMBL:OLB53330.1, ECO:0000313|Proteomes:UP000186629};
RN [1] {ECO:0000313|EMBL:OLB53330.1, ECO:0000313|Proteomes:UP000186629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLB53330.1}.
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DR EMBL; MNDS01000211; OLB53330.1; -; Genomic_DNA.
DR Proteomes; UP000186629; 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}.
FT DOMAIN 23..421
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 792..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1513 AA; 165809 MW; 3B3F2214D7C6699D CRC64;
MYVRSEIDPE YPLYDPRWEH DACGTGFIAQ VSGDASHYLV QTALQALANL THRGAQDADA
ETGDGAGLLT QIPKNLFYED LLARHITAAD LDDLAVGMIF LPSQERFPIS NIQCRHIIEQ
TLNEVGLMLL SWRNPPIDYS LLGSRARETA PSIAQVVLKC PRHLTAQQND GKLYHARRLI
EQRLEQARMK DCYIVSLSRT TIVHKGLLAP SELPHFYLDL LDPRYTSAFA IFHQRYSTNT
FPSWSLAQPT RQLAHNGEIN TIRGNLHWMK AREGTFFSPF WGSRMKDLLP VIQPGGSDSA
QLDDALELLT HSGRDLLQSV QMLIPPAWEQ DAELTSEQRA WCEFHAGITE PWDGPAALVF
SDGHYVGAAL DRNGLRPARY TLTSQGLLIL ASEAGVVPLE AHDVVEKGRL GPGEMIAVDL
QHGVLMRNSE IKTVLAQRQP YQRWLERYLV RLADITQSSA PLVEASLDPA ELFFRQQLFG
YTHEDVEFVL RPMLTERKEP IWSMGDDTPL AALSLHSRDL SDYFQQRFAQ VTNPPIDPLR
ERGVMSLDCY LGRRQNFLTE SALHAQLIHL ESPLLNESQL RIIGNLKADG FRTRTLNATF
ETAAGAVGFE AALERLEKEA VSAVADGATL LIVSDRTANP AFAPVPMLLA VGAIHQTLVR
QGLRTYISLL CETAAAWNIH QVALLLGYGA EAVVPYLALA SVRALAGERH LEHLTGEQAA
ELYLHVVEEG LRKVMARMGI STLRNIIGAG QFEIAGLDKA VLNRCFTGFS AHPGSVGFTQ
VAQQVIERCQ GLEQPAERQE DSAASGRRNK LRDSGRYRFR RDAEYHAFNP LLVKTLQKAA
LSGESEDYQR FTSMVYQRPP TALRDLFTFT ETTPISLEEV ESMEAIRARF VASAMSVGAL
SSEAHRTIAA AMNSIGGRNN TGEGGEDPDW YHEDMNGYPV SSKIKQVASA RFGVTTEYLV
RAEELEIKMA QGSKPGEGGQ LPPIKVTQFI ARLRHTAPQV ALISPPPHHD IYSIEDLAQL
IYDLRQVNPQ ARIGVKLVAS SGVGTIAAGV AKAHADYVLI SGHDGGTGAS PLQSIKHAGI
SWERGLAETQ QVLLRNGLRD RIKVRVDGGF KTGRDVIIGA MLGAEEFGFG TAILVAIGCD
MARQCHLNTC PTGIATQRED LRAKFTGRTE HITRYLTLLA EEVREWLARL GVARLDDLIG
RADLLQCTAE AIIDPSALLV AAPGTSSRST RVRQPQSALA EELLVEAEQA LLGERSVVTQ
HQIHNYDRAI GAGLAGEIAR RYGNAGLPGV SITCILQGAA GQSFGAFCLP GMRLVLHGEA
NDYVGKSMTG GQIIIAPPTD SSFAAHRNTI LGNTVLYGAT GGQLFAAGRA GERFAVRNSG
ALAVVEGVGA HACEYMTGGM VVVLGETGKN FAAGMSSGVA YVLDTAGVFP MRCNTELVEL
ERLDDAGEIE ALRTVIQWHG KKTRSWRAAQ LLAEWTRMQR VFWRVSPRGS VCTASDFVES
EDYDAAMVRV PQR
//
