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Database: UniProt
Entry: A0A1B9D4F3_MYCMA
LinkDB: A0A1B9D4F3_MYCMA
Original site: A0A1B9D4F3_MYCMA 
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
//
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