ID A0A1B9D4F3_MYCMA Unreviewed; 1527 AA.
AC A0A1B9D4F3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Glutamate synthase subunit alpha {ECO:0000313|EMBL:OCB49905.1};
GN ORFNames=A5677_24185 {ECO:0000313|EMBL:OCB49905.1};
OS Mycobacterium malmoense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1780 {ECO:0000313|EMBL:OCB49905.1, ECO:0000313|Proteomes:UP000092683};
RN [1] {ECO:0000313|EMBL:OCB49905.1, ECO:0000313|Proteomes:UP000092683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3012 {ECO:0000313|EMBL:OCB49905.1,
RC ECO:0000313|Proteomes:UP000092683};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
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:OCB49905.1}.
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DR EMBL; MBEE01000172; OCB49905.1; -; Genomic_DNA.
DR RefSeq; WP_065471807.1; NZ_MBEE01000172.1.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000092683; 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; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
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..416
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1527 AA; 166548 MW; 915A5D5CEBCF81E4 CRC64;
MTPKRVGLYN PAFEHDSCGV AMVVDMHGRR SRDIVDKAIT ALLNLEHRGA QGAEPRSGDG
AGILIQVPDA FLREVVDFEL PEPGSYATGI AFLPQSAKDA AAACDAVEKI AEAEGLTVLG
WRNVPIDDSS LGALSRDAMP TFRQVFLAGA SDMTLERRCY LVRKRAEHEL GTKGPGQDGP
GRETVYFPSL SGQTLVYKGM LTTPQLKAFY LDLQDDRMTS ALGIVHSRFS TNTFPSWPLA
HPFRRVAHNG EINTVTGNEN WMRAREALIK TEIFGTEADV EKLFPICTPG ASDTARFDEA
LELLHLGGRS LAHAVLMMIP EAWERNESMD PARRAFYEYH ASLMEPWDGP ASITFTDGTI
VGAVLDRNGL RPSRIWVTED GLVVMASEAG VLDLDPAKVV RRMRLQPGRM FLVDTTQGRI
VADEEIKAEL AAEHPYQEWL DRNLVPLEKL PQGDYTRMPH ERLVKRQLTF GYTYEELNLL
VSPMVRTGAE PIGSMGTDTP VAVLSQRPRM LYDYFQQLFA QVTNPPLDAI REEVVTSLQG
TTGGERDLLT PTEHSCHQIA LQQPILRNHE LAKLVNLNPD DEVNGRPHGM RSTVIRCLYP
VAEGGAGLAA ALDDVRAQAS AAIEDGARVI ILSDRESDER MAPIPSLLAV AGVHHHLVRD
RTRTHVGLVV ETGDAREVHH MAMLIGCGAA AINPYLAFES IEDMLDRGAI DGIDREKALN
NYVKAAGKGV LKVMSKMGIS TLASYTGAQL FQAVGISEDV LDEYFTGLSC PIGGITLEDI
AADVAARHRL AYLDRRDERA HRELEVGGEY QWRREGEYHL FNPETVFKLQ HSTRTGQYKI
FKDYTRLVDD QSERMASLRG LLKFRGGVRP PVPLDEVEPA SEIVKRFSTG AMSYGSISAE
AHETLAIAMN RLGGRSNSGE GGEDVKRFDR DKNGDWRRSA IKQVASARFG VTSHYLTNCT
DIQIKMAQGA KPGEGGQLPG HKVYPWVAEV RHSTPGVGLI SPPPHHDIYS IEDLAQLIHD
LKNANPSARV HVKLVSENGV GTVAAGVSKA HADVVLISGH DGGTGATPLT SMKHAGAPWE
LGLAETQQTL LLNGLRDRIV VQVDGQLKTG RDVMIAALLG AEEFGFATAP LVVAGCIMMR
VCHLDTCPVG VATQNPLLRE RFTGKPEFIE NFFMFIAEEV REYMAQLGFR TLNEAVGQVG
ALDTTLARAH WKAHKLDLAP VLHEPESAFM NQDLYCSSRQ DHGLDKALDQ QLIVMSREAL
DSGKPVRFST TISNVNRTVG TMLGHEVTKA YGGQGLPDGT IDITFDGSAG NSFGAFVPKG
ITLRVYGDAN DYVGKGLSGG RIVVRPSDNA PQDYVAEDNI IGGNVILFGA TSGEAFLRGV
VGERFAVRNS GAHAVVEGVG DHGCEYMTGG RVVILGRTGR NFAAGMSGGV AYVYDPDEEL
PDNLNIEMVD MEAPDSDDAE FLHGIIQAHV DATDSAVGQR ILADWRGQQR HFVKVMPRDY
KKVLQAIAEA ERDGTDVDKA IMAAAHG
//