ID Q745H0_MYCPA Unreviewed; 1527 AA.
AC Q745H0;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=GltB {ECO:0000313|EMBL:AAS02489.1};
GN Name=gltB {ECO:0000313|EMBL:AAS02489.1};
GN OrderedLocusNames=MAP_0172 {ECO:0000313|EMBL:AAS02489.1};
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316 {ECO:0000313|EMBL:AAS02489.1, ECO:0000313|Proteomes:UP000000580};
RN [1] {ECO:0000313|EMBL:AAS02489.1, ECO:0000313|Proteomes:UP000000580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580};
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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}.
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DR EMBL; AE016958; AAS02489.1; -; Genomic_DNA.
DR RefSeq; WP_010948765.1; NZ_CP106873.1.
DR STRING; 262316.MAP_0172; -.
DR MEROPS; C44.003; -.
DR KEGG; mpa:MAP_0172; -.
DR PATRIC; fig|262316.17.peg.179; -.
DR eggNOG; COG0067; Bacteria.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG0070; Bacteria.
DR HOGENOM; CLU_000422_8_2_11; -.
DR Proteomes; UP000000580; Chromosome.
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:UP000000580}.
FT DOMAIN 18..416
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 1527 AA; 166234 MW; C3AEBE30B8C2B605 CRC64;
MTPKRAGLYN PAFEHDACGV AMVVDMHGRR SRDIVDKAIT ALLNLEHRGA QGAEPRSGDG
AGILIQVPDA FLREVVDFEL PPEGSYATGI AFLPQSSKDA ATACAAVEKI AEAEGLTVLG
WRNVPTDDSS LGALSRDAMP TFRQVFMAGA SGMTLERRAY LMRKRAEHEL GTKGPGQDGP
GRETVYFPSL SGQTFVYKGM LTTPQLKAFY LDLQDDRLTS ALGIVHSRFS TNTFPSWPLA
HPFRRIAHNG EINTVTGNEN WMRAREALIK TDVFGTEADV EKLFPICTPG ASDTARFDEV
LELLHLGGRS LAHAVLMMIP EAWERHESMD PARRAFYQYH ASLMEPWDGP ASMTFTDGTV
IGAVLDRNGL RPSRIWVTED GLVVMASEAG VLDLDPATVV RRMRLQPGRM FLVDTAQGRI
VSDEEIKAEL AAEHPYQEWL DRNLVPLDDL PQGDYKRMPH DRLVKRQQTF GYTYEELNLL
VAPMVRTGAE PIGSMGTDTP VAVLSQRPRM LYDYFQQLFA QVTNPPLDAI REEVVTSLQG
TTGGERDLLT PTELSCHQIV LSQPILRNRE LAKLVNLNPD DEVNGRPHGM RSKVIRCLYP
VAEGGAGLAA ALEDVRAQAS AAIADGARVI ILSDRESDEK MAPIPSLLAV AGVHHHLVRD
RTRTHVGLVV ESGDAREVHH MAALVGFGAA AINPYMVFES IEDMLDRGVI EGIDRNTALN
NYVKAAGKGV LKVMSKMGIS TLASYTGAQL FQAVGISEDV LDEYFTGLSC PIGGITLDDI
AADVAARHAL AYLDRPNERA HRELEVGGEY QWRREGEYHL FNPETVFKLQ HATRTGQYKI
FKDYTRLVDD QSERMASLRG LLKFRAGVRP PVPLEEVEPA SEIVKRFSTG AMSYGSISAE
AHETLAIAMN RLGGRSNSGE GGEDVKRFDR DPDGSWRRSA IKQVASGRFG VTSHYLTNCT
DIQIKMAQGA KPGEGGQLPG HKVYPWVAEV RHSTPGVGLI SPPPHHDIYS IEDLAQLIHD
LKNANPAARV HVKLVSENGV GTVAAGVSKA HADVVLISGH DGGTGATPLT SMKHAGAPWE
LGLAETQQTL LLNGLRDRIV VQVDGQLKTG RDVMIAALLG AEEFGFATAP LVVSGCIMMR
VCHLDTCPVG VATQNPVLRE RFTGKPEFVE NFFMFIAEEV REYMAQLGFR TLNEAVGQVK
SLDTTLARAH WKAHRLDLGP VLHEPESAFM NQDLYCSSRQ DHGLDKALDQ QLIVMSREAL
DSGKPVRFST TISNVNRTVG TMLGHEVTKA YGGQGLPDGT IDITFDGSAG NSFGAFVPRG
ITLRVYGDAN DYVGKGLSGG RIVVRPSDNA PADYVAEDNI IGGNVILFGA TSGEAYLRGV
VGERFAVRNS GAHAVVEGVG DHGCEYMTGG KVVVLGRTGR NFAAGMSGGV AYIYDPPGEF
PQHLNAEMVE LESLDDDDIE WLHGMIQAHV DATDSAVGQR ILGDWAQQQR HLVKVMPRDY
KRVLQAIAEA ERDGGDVDKA IMAAAHG
//
