ID A1WVX0_HALHL Unreviewed; 1486 AA.
AC A1WVX0;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Glutamate synthase (NADPH) large subunit {ECO:0000313|EMBL:ABM61832.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:ABM61832.1};
GN OrderedLocusNames=Hhal_1056 {ECO:0000313|EMBL:ABM61832.1};
OS Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS halophila (strain DSM 244 / SL1)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=349124 {ECO:0000313|EMBL:ABM61832.1, ECO:0000313|Proteomes:UP000000647};
RN [1] {ECO:0000313|Proteomes:UP000000647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA Richardson P.;
RT "Complete sequence of Halorhodospira halophila SL1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABM61832.1, ECO:0000313|Proteomes:UP000000647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RX PubMed=23991253; DOI=10.4056/sigs.3677284;
RA Challacombe J.F., Majid S., Deole R., Brettin T.S., Bruce D., Delano S.F.,
RA Detter J.C., Gleasner C.D., Han C.S., Misra M., Reitenga K.G.,
RA Mikhailova N., Woyke T., Pitluck S., Nolan M., Land M.L., Saunders E.,
RA Tapia R., Lapidus A., Ivanova N., Hoff W.D.;
RT "Complete genome sequence of Halorhodospira halophila SL1.";
RL Stand. Genomic Sci. 8:206-214(2013).
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; CP000544; ABM61832.1; -; Genomic_DNA.
DR RefSeq; WP_011813855.1; NC_008789.1.
DR STRING; 349124.Hhal_1056; -.
DR MEROPS; C44.003; -.
DR KEGG; hha:Hhal_1056; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_6; -.
DR Proteomes; UP000000647; Chromosome.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) 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:ABM61832.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000647}.
FT DOMAIN 19..410
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1486 AA; 161992 MW; 943EA503A94A0D96 CRC64;
MTDENAPGLY RPSFERDNCG FGLIAHMDGN PSHWLIETAV AALGRLTHRG AVAADGKTGD
GCGLLLTKPD AFLRAVAHEA GLDLDEQFAV GSLFLHPEEG FAEAAREALR QALRSQGLEP
AGFREVPVDT SALGAQALQT CPRIEQAFVN ADPGMEAQDL ERRLFIARRL TEKAISSEDE
VFYVASLSGR VLSYKGLVMP DYLPAFYQDL QDPRLASSLC VFHQRFSTNT LPQWRLAQPF
RYLAHNGEIN TIQGNRNWAN ARAFTLNTPL IPDMEAVHPL VNSEGSDSSS LDNMLDVLLQ
GGMDIFRAMR LLMPPAWQNV DSMDADLRAF YEYHSMHCEP WDGPAGIVLT DGRHAACSLD
RNGLRPARWV MTRDRHITLA SEIGVWDYDP AEVVAKGRLK PGEMLAADTE TGQLLTPEQI
DERLMRRKPY KAWLSEHLRR LEPLAGFDGK SPQLDQNALD VHQKLFGISF EERDQVMKPM
AEGGQEAVGS MGDDTPLPVL SRRVRALYDT FRQQFAQVTN PAIDPLRERI VMSLETCLGR
EKNLFDESED HAKRITVDSP VLSGAKFAAI KALDDPEYAH TVIDLTYDPS QLNLRSAIEA
VAAEAEAAVR AGSTLVVLSD RRVERGRLTI HALLATGAVH HRLVARGLRC NANLIVETGT
ARDPHHIGCL IGYGATCVYP YLAYEVVAEM ARSGRMEGDV EALCLNYRKG LNKGLYKILS
KMGISTIASY RGAQLFESVG LADEVVDLCF TGTTNRIQGM NFSDLEADAR ELARRAHRAT
ELLDQGGVFK YVHGGEYHCY NPEVVSYLQQ AVEDGDYATY KRFADAVNQR PTATLRDLLG
LKVPDQGIAV DEVQPIDDIL TRFDSAGMSL GALSPEAHEA LAMAMNRLGG RSNSGEGGED
PARYGTDRVS KIKQIASGRF GVTPHYLVNA EVLQIKVAQG AKPGEGGQLP GHKVNEMIAR
LRYSKPGVAL ISPPPHHDIY SIEDLAQLIF DLKQVNPEAQ VSVKLVAEAG VGTVAAGVAK
AYADLITIAG YDGGTGASPL TSVKYAGGPW ELGLTETHQT LRANDLRDKV RLQADGGMKT
GLDVVKGAIL GAESFGFGTA PMVALGCKYL RICHLNNCAT GVATQDNVLR LKHFVGTAEK
VANYFRFVAE ETREWLALLG VRRLEDLIGR TDLLEVLPGE TERQGRLDLS PILSDGGVPE
DKPKRCLEPS NVPFDKGELA EQMVADCLPT IEAGSGGEFH YTLRNNNRSI GARLSGEIAR
RHGNQGMADH PITLRLTGTA GQSFGVWNAG GLHMVLEGDA NDYVGKGMAG GKLVLYPPQG
SRFEARKTTI MGNTCLYGAT GGRLYAAGTV GERFGVRNSG ATAVVEGVGD HGCEYMTGGV
VCVLGPTGVN FGAGMTGGLA FVLDEAGTFA DRYNHELIDI HRLQSENMEA HRNYLRELIR
EFVAETGSVW GRAVLDDFRG YLPRFWLVKP KAADLHTILD TLRQAA
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