ID A0A0D1EDV6_9RHOB Unreviewed; 1512 AA.
AC A0A0D1EDV6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=GltB protein {ECO:0000313|EMBL:KIT15121.1};
DE EC=1.4.1.13 {ECO:0000313|EMBL:KIT15121.1};
GN Name=gltB {ECO:0000313|EMBL:KIT15121.1};
GN ORFNames=jaqu_34490 {ECO:0000313|EMBL:KIT15121.1};
OS Jannaschia aquimarina.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=935700 {ECO:0000313|EMBL:KIT15121.1, ECO:0000313|Proteomes:UP000032232};
RN [1] {ECO:0000313|EMBL:KIT15121.1, ECO:0000313|Proteomes:UP000032232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSW-M26 {ECO:0000313|EMBL:KIT15121.1,
RC ECO:0000313|Proteomes:UP000032232};
RA Voget S., Daniel R.;
RT "Genome Sequence of Jannaschia aquimarina DSM28248, a member of the
RT Roseobacter clade.";
RL Submitted (FEB-2015) 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:KIT15121.1}.
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DR EMBL; JYFE01000060; KIT15121.1; -; Genomic_DNA.
DR RefSeq; WP_043920176.1; NZ_JYFE01000060.1.
DR STRING; 935700.jaqu_34490; -.
DR PATRIC; fig|935700.4.peg.3558; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000032232; Unassembled WGS sequence.
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:KIT15121.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032232}.
FT DOMAIN 34..430
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 912..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1512 AA; 163942 MW; 218692C5AA74ACA5 CRC64;
MTHWFTEFER DELARRAEMG ETSLYREEAE HASCGVGLVV DIKGRKSRKV VESGIQALKA
IWHRGAVDAD GKTGDGAGIH VQIPVEFFQD QVRRTGHEPS KGLLAVGQVF LPRTDFGAQE
VCRTIVETEV LRMGYGIYGW RHVPVNIDVL GEKANATRPE IEQILIRDTK GVDEETFERE
LYVIRRRIEK AAAAAQVPGL YLASLSCRSI IYKGMMLAEQ VAEFYPDLKD ERFESAFAIY
HQRYSTNTFP QWWLAQPFRM LAHNGEINTL KGNVNWMRSH EIRMASSAFG DLAGDIKPIV
PPGASDSAAL DSVFEVLVRA GRNAPMAKTM LVPESWSKQA VELPEAWRDM YSYCNSVMEP
WDGPAALAMT DGRWVCGGLD RNGLRPMRYV VSGEGLLIAG SEVGMVPTDE AAVIEKGALG
PGQMIAVDMA EGKLFHDGEI KDKLAASQPF GDWVERITDL EEVTKGVSET AIHSGEELRR
RQIAAGYSIE ELEQILAPMA EDGKETVASM GDDTPAAVLS EKYRPLSHFF RQNFSQVTNP
PIDSLREYRV MSLKTRFGNL KNVLDEDSSQ TEILVLDSPF VGNSQFESIM DQMGDAVVTI
DCTFAAGAEK GALAAGLTRI RDEAEEAVRS GAGHIVLTDR FQSEDKVPMP MILATSAVHS
WLTRKGLRTF CSLNVRSAEC IDPHYFAVLI GCGATTVNPY LAQDSLADRI DRGLLEGTLT
EAVARYRKAV DAGLLKIMSK MGISVISSYR GGLNFEAVGL SRAMVAEYFP GMLSRISGIG
VIGLQSQVEA VHGRGWLGQA QNVLPIGGFY KARRQGEKHA WEAQTMHMLQ SACDRASYEM
WKQYSTALQK NPPIHLRDLL AIKPLGKAIP LEEVESITSI RKRFVTPGMS LGALSPEAHK
TLNVAMNRIG AKSDSGEGGE DPAHFVPEPN GDNPSAKIKQ VASGRFGVTA EYLNHCEELE
IKVAQGAKPG EGGQLPGMKV TKLIARLRHS TPGVTLISPP PHHDIYSIED LAQLIYDLKQ
INPRCKVTVK LVASSGVGTI AAGVAKAKAD VILISGHNGG TGASPATSIK YAGLPWEMGL
TEAHQVLAMN KLRERVTLRT DGGLRTGRDI VMAAMMGAEE YGIGTAALIA MGCIMVRQCQ
SNTCPVGVCT QDPALREKFT GTADKVVNLI TFYAQEVREI LAEIGARSLD EVIGRADLLT
QVSRGSAHLD DLDLNPLLIT VDGADRIELD RGKPRNAVPD TLDAQIVTDA ARFLEDGEKM
QLSYAVQNTH RTVGTRLSSH IVKRFGMRNS LQPDHLHVKL TGSAGQSLGA FAAPGLKLEV
SGDANDYVGK GLSGGTIVVR PPQVSPLRAD ENVIIGNTVL YGATDGYLFA AGRAGERFAV
RNSGAKVVVE GCGSNGCEYM TGGVAVILGE IGANFGAGMT GGMAYVHDPD GTALELMNLE
TLVTNPVTVA HWEGQLRGLI ERHAAETNSR KAKAILADWD LELGNFVQVC PTEMLPHLAA
PLSEEADAVP AE
//
