ID   FLUG_EMENI              Reviewed;         865 AA.
AC   P38094; C8VAB0; Q5B3R1;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Protein fluG;
GN   Name=fluG; Synonyms=acoD; ORFNames=AN4819;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FGSC 26;
RX   PubMed=7926755; DOI=10.1101/gad.8.6.641;
RA   Lee B., Adams T.H.;
RT   "The Aspergillus nidulans fluG gene is required for production of an
RT   extracellular developmental signal and is related to prokaryotic glutamine
RT   synthetase I.";
RL   Genes Dev. 8:641-651(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: May function as a GSI-related enzyme in synthesizing a small
CC       diffusible factor that acts as an extracellular signal directing
CC       asexual sporulation and perhaps other aspects of colony growth. May be
CC       involved in brlA activation (an early transcriptional regulator for
CC       conidiation specific gene).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; L27817; AAC37414.1; -; Genomic_DNA.
DR   EMBL; AACD01000081; EAA60389.1; -; Genomic_DNA.
DR   EMBL; BN001303; CBF76713.1; -; Genomic_DNA.
DR   PIR; A53186; A53186.
DR   RefSeq; XP_662423.1; XM_657331.1.
DR   AlphaFoldDB; P38094; -.
DR   SMR; P38094; -.
DR   STRING; 162425.CADANIAP00005600; -.
DR   EnsemblFungi; CBF76713; CBF76713; ANIA_04819.
DR   EnsemblFungi; EAA60389; EAA60389; AN4819.2.
DR   GeneID; 2872617; -.
DR   KEGG; ani:AN4819.2; -.
DR   VEuPathDB; FungiDB:AN4819; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   HOGENOM; CLU_017290_6_3_1; -.
DR   InParanoid; P38094; -.
DR   OMA; LEGCPRT; -.
DR   OrthoDB; 142334at2759; -.
DR   Proteomes; UP000000560; Chromosome III.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IDA:AspGD.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0001896; P:autolysis; IMP:AspGD.
DR   GO; GO:0048315; P:conidium formation; IMP:AspGD.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   GO; GO:0075307; P:positive regulation of conidium formation; IMP:AspGD.
DR   GO; GO:0010914; P:positive regulation of sterigmatocystin biosynthetic process; IMP:AspGD.
DR   GO; GO:1900376; P:regulation of secondary metabolite biosynthetic process; IMP:AspGD.
DR   GO; GO:0010913; P:regulation of sterigmatocystin biosynthetic process; IMP:AspGD.
DR   GO; GO:0000905; P:sporocarp development involved in asexual reproduction; IMP:AspGD.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   GO; GO:0045461; P:sterigmatocystin biosynthetic process; IMP:AspGD.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF04909; Amidohydro_2; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   PROSITE; PS51986; GS_BETA_GRASP; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   1: Evidence at protein level;
KW   Conidiation; Cytoplasm; Reference proteome; Sporulation.
FT   CHAIN           1..865
FT                   /note="Protein fluG"
FT                   /id="PRO_0000153281"
FT   DOMAIN          442..533
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          540..865
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   MUTAGEN         774
FT                   /note="Y->N: Temperature-sensitive."
SQ   SEQUENCE   865 AA;  96505 MW;  D17F3BB83B8F1719 CRC64;
     MATLSSLRHL IQTHPLIDNH AHNLLSQSAA CKYAKYPFEQ IISEAQGVAL ANAPSTLSFH
     RAASQLATLY QSSSSDWDSV RAARDQSVQR DYEGLIRKCL EGTQVLLLDD LLTENDVELF
     DWHDRFTASA TKRIVRIEAL AASVLSQIVH GGPVPQDSSD LSAFQTLWES FSRNFSALVS
     DAIADPAVVG FKSVICYRTG LDVQPTDDRD TERLIRSFAR TISQAAVSTP RVEDKPLNDW
     LVRQTLNLLK AAKVTQPNKP LQLHTGLGDN DINLLKSNPA HLQSLIAQYP EVDFVLLHSS
     YPYTREAGYL ACVYPNVYLD LGEVFPMVSR DAQESILRES LEIVPSTRLL WSTDGHFFPE
     TFWLANRQFR DALEKVFVDY VQNGDYTIEQ AMQAAADILF HNSNRLYELN EQPPSAALSS
     GHQTVSRISS TDLLEKFIRS NPGVKYVWTQ FIDYTATVRV RMFPVMEFAK IVRKQRRLGI
     SMATFWMLQD DEVVGGSTTG QFYLIPDLST LSPNVGIDSK SATVMTWWKS EQGESLEECP
     RTNLLNINNK LKDEFGIQAT CGFEIEVVFL KPTTDPSTGE EDWAPSVTNH SWSQMTRETR
     RMLPLLEEIA ETLASIGIHL QQFHAESAPG QFEFILPPDN PVAAVDTLIK SRQVIANIVE
     KHGLRATLYP RPYPSAAGTA SHAHVSISPS TKEESFLAGV LQHYPAVLAF TLSGDASYDR
     VKSGIWAGSE WVTWGTQNRE APIRKISPGH WEIKSLDGLA NMYLAMAAFL AAGYTGVKEN
     LPLTIKDCPY DAASLPESER AALGITTKLP NTLAKSLAAL ESDEILRSLL GENLVEDYII
     VKRAESKKLS AMDEKARRKW LVERY