ID A0A1G7X9E0_9ACTN Unreviewed; 1504 AA.
AC A0A1G7X9E0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glutamate synthase (NADPH/NADH) large chain {ECO:0000313|EMBL:SDG80200.1};
GN ORFNames=SAMN05421505_10873 {ECO:0000313|EMBL:SDG80200.1};
OS Sinosporangium album.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Sinosporangium.
OX NCBI_TaxID=504805 {ECO:0000313|EMBL:SDG80200.1, ECO:0000313|Proteomes:UP000198923};
RN [1] {ECO:0000313|EMBL:SDG80200.1, ECO:0000313|Proteomes:UP000198923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 201354 {ECO:0000313|EMBL:SDG80200.1,
RC ECO:0000313|Proteomes:UP000198923};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FNCN01000008; SDG80200.1; -; Genomic_DNA.
DR STRING; 504805.SAMN05421505_10873; -.
DR OrthoDB; 9758182at2; -.
DR Proteomes; UP000198923; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198923}.
FT DOMAIN 24..410
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 311..346
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
SQ SEQUENCE 1504 AA; 162103 MW; 3050D99706271CEC CRC64;
MPAARSGIPE PQGLYHPSHE HDACGVAMVA DVHGRRSHDI VRKALTALTN LDHRGAKGSE
PDTGDGAGIL TQIPDALFRE VVDFALPGPG AYAAGTAFLP ADGQAREIAV RMIEEIAAEE
GLTVLGWRDV PIDPAYAGPS ARAVMPFFAQ IFVSSPNGET GLALDRPAFC LRKRAEHEVD
VYFPSLSSRT VVYKGMLTTP QLEPFFPDLS DERYATAISL VHSRFSTNTF PSWPLAHPYR
YVAHNGEINT VKGNRNWMRA REAMLASDLI PGDLRRLFPI CDPDGSDTAS LDETLELLHL
GGRSLPHAVL MMVPEAWENH TEMDPARRAF YEFHSTLMEA WDGPASITFS DGTLVGALLD
RNGLRPGRFY VTDDGLVVLA SEAGVLDIPQ HKVVRKGRLQ PGRMFLVDTA QGKIIEDGEI
KAELAAAQPY AGWLHAGLVR FEELPSRSRE IPTHEALVRR QQTFGYTEEE LRVILAPMAK
TGYEPIGSMG TDTPVAVLSE RPRLLFDYFS QLFAQVTNPP LDAIREELVT SLQSTIGPER
NLLDPGAASC RRLVLPYPVI DNDELAKIIH INDEGALPGF QPYVVSGLYD IAGGGEALTA
RLEAICTEVS EAIKGGARTI VLSDRGSSAE SAPIPSLMLT GAVHHHLIRE KSRTRVGLVV
ETGEARECHH MALLIGYGAS AVNPYLAIET VEDMIATGEL SLDPRKAVRN LIKAYGKGVL
KVMSKIGVST VASYTGAQIF EALGLGQEVV DACFTGTTSR LGGVGFDVLS RETAERHRRA
YPRAENAHRR LEVGGEYQWR REGEPHLFNP ETVFRLQHST RTGRYEIFKE YTTLVDSQAE
KLMTLRGLFK FREGARPPVP IEEVEPVSEI VKRFSTGAMS YGSISREAHE TLAIAMNRLG
AKSNTGEGGE DPDRLYDPVR RSAIKQVASG RFGVTSEYLV NADDVQIKMA QGAKPGEGGQ
LPGNKVYPWI AKTRHSTPGV GLISPPPHHD IYSIEDLAQL IHDLKNANPA ARVHVKLVAE
VGVGTVAAGV SKAHADVVLI SGHDGGTGAS PLTSVKHAGA PWELGLAETQ QTLLLNGLRD
RIVVQVDGQL KTGRDVVIAA LLGAEEYGFA TAPLVVSGCV LMRVCHLDTC PVGVATQNPE
LRKRFSGKPE FVVNFFEFIA EEVREYLAAL GFRSLDEAVG HAELLDTERA EGHWKAAGLD
LSPILHMPEL PAGTPLHQVV TQDHGLAHAL DNTLIQLAEG ALEYGSPVKL ELPIRNVNRT
VGTMLGHEVT KRYGGAGLPA NTIDVAFTGS AGNSFGAFVP KGVTLRLTGD ANDYLGKGLS
GGRITVRPPA DAAFAAETQV IAGNVGLYGA TSGEVFLRGI VGERFCVRNS GATAVVEGVG
DHGCEYMTGG RAVVLGPTGR NFAAGMSGGV AYVLDLVPER VNREMVELEE PTGEDADFLR
EVVEAHFTET GSAVASALLA DWDAALTRFA KIMPRDFKRV LAARAAAEAE GRDIDEAVMA
AAQG
//
