ID A0A1A2ZTP9_9MYCO Unreviewed; 1530 AA.
AC A0A1A2ZTP9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:OBI53680.1};
GN ORFNames=A5707_11220 {ECO:0000313|EMBL:OBI53680.1};
OS Mycobacterium kyorinense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=487514 {ECO:0000313|EMBL:OBI53680.1, ECO:0000313|Proteomes:UP000093592};
RN [1] {ECO:0000313|Proteomes:UP000093592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E861 {ECO:0000313|Proteomes:UP000093592};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Sam S., Sreng N.,
RA Him V., Kerleguer A., Cheng S.;
RL Submitted (JUN-2016) 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:OBI53680.1}.
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DR EMBL; LZKJ01000006; OBI53680.1; -; Genomic_DNA.
DR RefSeq; WP_065012552.1; NZ_LZKJ01000006.1.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000093592; 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 InterPro; IPR001202; WW_dom.
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.
DR PROSITE; PS50020; WW_DOMAIN_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 18..419
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 320..355
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
SQ SEQUENCE 1530 AA; 165851 MW; B981A4DE0AD613F7 CRC64;
MAPNRVGLYN PAFEHDSCGV AMVVDMHGRR SRDIVEKAIT ALLNLEHRGA AGAEPHSGDG
AGILIQVPDD FLRAIVDFEL PAAGSYATGI AFLPQSSKDA AAACAAVEKI VASEGLKVLG
WRDVPTDDSS LGALSRDAMP TFRQLFVAGA SGMELERRAY VIRKRAEHEL GTKGPGQDGP
GRETVYFASL SGQTFVYKGM LTTPQLKAFY LDLQDDRLTS ALGIVHSRFS TNTFPSWPLA
HPFRRIAHNG EINTVTGNEN WMRAREALIR TDVFGEPGDL DSADKLFPIC TPGASDTARF
DEVLELLHLG GRSLAHAVLM MIPEAWERHE SMDPARRAFY AYHSSLMEPW DGPASMTFTD
GTIIGAVLDR NGLRPSRIWV TDEGLVVMAS EAGVLDLDPS TVVRRMRLQP GRMFLVDTAQ
GRIVSDEEIK AELAAEHPYQ EWLDKGLIPL EELPQGNYVQ MPHHRVVLRQ LVFGYTYEEL
NLLVAPMVRT GAEPLGSMGT DTPVAVLSER PRMLFDYFQQ LFAQVTNPPL DAIREEVVTS
LHGALGPEGD LLNPTEDSCR QIVLSQPILR NHELAKLINL DPDVEVNGRR HGLRSTVIRC
LYPVNEGGAG LKAALDDVRS QTSAAIADGA RIIILSDRES DQEMAPIPSL LAVSAVHHHL
VRERSRTKVG LVVESGDARE VHHMAALVGF GAAAINPYMA FESIADMLDR GAITGIELEK
ALQNYIKAAG KGVLKVMSKM GISTLASYTG AQLFQAVGVS EDLLDEYFTG LTCPTGGITL
DDIAADVATR HALAFLDRPD ERAHRELEVG GEYQWRREGE YHLFNPDTVF KLQHSTRTGQ
YKIFKEYTRL VDDQSERMAS LRGLLKFRDG FRPPVPLDEV EPATEIVKRF ATGAMSYGSI
SAEAHETLAV AMNRLGGRSN SGEGGEHIGR FDRDPNGDWR RSAIKQVASA RFGVTSHYLT
NCSDIQIKMA QGAKPGEGGQ LPGGKVYPWI AEVRHSTPGV GLISPPPHHD IYSIEDLAQL
IHDLKNANPS ARIHVKLVSE NGVGTVAAGV SKAHADVVLI SGHDGGTGAT PLTSMKHAGA
PWELGLAETQ QTLLLNGLRD RIVVQVDGQL KTGRDVMIAA LLGGEEFGFA TAPLVVSGCI
MMRVCHLDTC PVGVATQNPV LRQRFTGKPE FVENFFLFIA EEVREYMAAL GFRTLNEAVG
QVGALDTTLA RAHWKAHKLD LTPVLHEPES AFMNQDLYCS SSQDHGLDKA LDQQLIVMSR
EALDSGSPVR FSTTISNVNR TVGTMLGHEV TKAYGGQGLP DGTIDITFDG SAGNSFGAFV
PKGITLRVYG DANDYVGKGL SGGRIVVRPS DNSPEGYAAE DNIIGGNVIL FGATSGEAFL
RGVVGERFAV RNSGAYAVVE GVGDHGCEYM TGGKVVILGR TGRNFAAGMS GGVAYVYDPD
AVFPSHLNTE MVELEALDDE DLDWLHGIIQ AHVDATDSAV GQRILGDWAG EQRCFVKVMP
RDYKRVLEAI AEAERDGTDV DEAVMAAAHG
//
