ID A0A1A1ZAP5_9MYCO Unreviewed; 1529 AA.
AC A0A1A1ZAP5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:OBF40633.1};
GN ORFNames=A5724_07615 {ECO:0000313|EMBL:OBF40633.1};
OS Mycobacterium sp. ACS1612.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834117 {ECO:0000313|EMBL:OBF40633.1, ECO:0000313|Proteomes:UP000092025};
RN [1] {ECO:0000313|Proteomes:UP000092025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS1612 {ECO:0000313|Proteomes:UP000092025};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Kiyimba A., Mayanja H.,
RA Musoke P., Ssengooba W., Joloba M.;
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:OBF40633.1}.
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DR EMBL; LZHZ01000006; OBF40633.1; -; Genomic_DNA.
DR RefSeq; WP_067796486.1; NZ_LZHZ01000006.1.
DR STRING; 1834117.A5724_07615; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000092025; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000092025}.
FT DOMAIN 18..415
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1529 AA; 166144 MW; B4FA6B4E0B837E90 CRC64;
MAPSKQGLYN PAFEHDACGV AMVADMHGRR SRDIVDKAIT ALVNLEHRGA QGAEPHTGDG
AGILLQVPDE FLRAVVDFDL PEYGSYATGI AFLPQSSKDA AAACEAVEKI AEAEGLVVLG
WRDVPTDESS LGALARDAMP TFRQLFLAGA SGMDLERRAY VVRKRAEHEL GTKGPGQDGP
GRETVYFPSL SGQTFVYKGM LTTPQLKAFY LDLQDDRLTS ALGIVHSRFS TNTFPSWPLA
HPFRRIAHNG EINTVTGNEN WMRAREALIN TDLFGGRDLE KVTPICTPGA SDTARFDEVL
ELLHLGGRSL PHAVLMMIPE AWERNESMDP ARRAFYSYHA SLMEPWDGPA SMTFTDGTVI
GAVLDRNGLR PSRIWVTADG LVVMASEAGV LNLDPSTVVK KMRLQPGRMF LVDTSKGRIV
DDEEIKAELA AEQPYQEWLD AGLFRLEDLP PGDYVRMPHH RVVLRQQIFG YTYEELNLLV
APMARTGAEP IGSMGTDTPI AVLSQRPRML YDYFQQLFAQ VTNPPLDAIR EEVVTSLQGT
VGPEGDLLNP DAESCRQIVL PQPILRNAEL SKLMCVDPDH EIRGHKHGMR AAVIRCLYPV
NRGGQGLKEA LDNVRAKVSA AIRDGARIIV LSDRESDESM APIPSLLSVS AVHHHLVRDR
TRTKVGLVVE AGDAREVHHM ACLVGFGAAA INPYMAFESI EDMVDRGVIT GITSDQAKAN
YVKAAGKGVL KVMSKMGIST LASYTGAQLF QAIGISQPLL DEYFTGLTCP VGGIDLDDIA
GDVAARYALA YLDRPDEWAH RELEVGGEYQ WRREGEYHLF NPDTVFKLQH STRTGQYEVF
KEYTKLVDDQ SERMASLRGL LKFRDGVRPP VPLDEVEPAS EIVKRFSTGA MSYGSISAEA
HETLAIAMNR LGGRSNSGEG GEDVRRFEQD ENGDWRRSAI KQVASARFGV TSHYLTNCTD
IQIKMAQGAK PGEGGQLPGN KVYPWVAEVR HSTPGVGLIS PPPHHDIYSI EDLAQLIHDL
KNANPQARVH VKLVSENGVG TVAAGVSKAH ADVVLISGHD GGTGATPLTS QKHAGAPWEL
GLAETQQTLL LNGLRDRIVV QVDGQLKTGR DVVIAALLGA EEFGFATAPL VVSGCIMMRV
CHLDTCPVGV ATQNPVLRQR FAGKPEFVEN FFMFIAEEVR EMMAQLGFRT VNEMVGQVGA
LDTTQAAEHW KAYKLDLAPV LYEPESAFMN QDLYCSSRQD HGLDKALDQQ LIVMSREALD
SGTPVKFSTT IANTNRTVGT MLGHELTKAY GGQGLPDGTI DITFDGSAGN SFGAFVPKGI
TLRVYGDAND YVGKGLSGGR IVVRPSDDAP ADYVAEENII AGNVILFGAT SGQVFLRGVV
GERFAVRNSG AHAVVEGVGD HGCEYMTGGK VVILGPTGRN FAAGMSGGVA YVYNPDGTFE
QNLNAEMVDL DEIGGDDSDD GVWLRGMIQA HVDATDSAVG QRVLSDWENE LKNFTKVMPR
DFKRVLQAMA KAEQTGENVD EAIMAAANA
//
