ID A5DMF7_PICGU Unreviewed; 2679 AA.
AC A5DMF7;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=glutamate synthase (NADH) {ECO:0000256|ARBA:ARBA00024383};
DE EC=1.4.1.14 {ECO:0000256|ARBA:ARBA00024383};
GN ORFNames=PGUG_04458 {ECO:0000313|EMBL:EDK40360.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK40360.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK40360.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + L-glutamine +
CC NADH; Xref=Rhea:RHEA:13753, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58359; EC=1.4.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00024267};
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; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NAD(+)
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00004944}.
CC -!- PATHWAY: Energy metabolism; nitrogen metabolism.
CC {ECO:0000256|ARBA:ARBA00004802}.
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH408159; EDK40360.2; -; Genomic_DNA.
DR RefSeq; XP_001483729.1; XM_001483679.1.
DR STRING; 294746.A5DMF7; -.
DR GeneID; 5125096; -.
DR KEGG; pgu:PGUG_04458; -.
DR VEuPathDB; FungiDB:PGUG_04458; -.
DR eggNOG; KOG0399; Eukaryota.
DR HOGENOM; CLU_000422_8_2_1; -.
DR InParanoid; A5DMF7; -.
DR OMA; WDGPAAM; -.
DR OrthoDB; 20503at2759; -.
DR UniPathway; UPA00045; -.
DR UniPathway; UPA00634; UER00690.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0097054; P:L-glutamate biosynthetic process; IEA:UniProtKB-UniPathway.
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; 3.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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 Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
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; IPR006005; Glut_synth_ssu1.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR NCBIfam; TIGR01317; GOGAT_sm_gam; 1.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF00310; GATase_2; 1.
DR Pfam; PF04898; Glu_syn_central; 1.
DR Pfam; PF01645; Glu_synthase; 2.
DR Pfam; PF01493; GXGXG; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF69336; Alpha subunit of glutamate synthase, C-terminal domain; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 2.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW 3Fe-4S {ECO:0000256|ARBA:ARBA00023291};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
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};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997}.
FT DOMAIN 45..457
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 1489..1651
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT REGION 2140..2161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2679 AA; 295787 MW; 7932D10D624E20BB CRC64;
MSYLPHDEFE TNVYSYDEVP ENKSWASTLP TAKGLYNPEY EKDACGVGFT CHIKGQASHK
IVSDCRNLLC NMTHRGGELN PKDGDGAGLL SSLPHKFLVR EFQYHCNVTL PPLGQYGTGN
VFFKKDDVVF EKSKKTFENI AASLGLRVLG WRAVPHDSSI LGPASLSREP LILQPLIVLA
EAFGPGSAPQ EDISTDDFEK KYQRSFEKNL FILRKQSSHT IGLHNWFYIC SLSNRTIVYK
GQLAPNQVYA YYHDLVNADF EAHFALVHSR FSTNTFPSWD RAQPLRWAAH NGEINTLRGN
KNWMRAKEGV MASELFGDEL DKLYPIIEEG GSDSAAFDNV LELLVINGVL SLPEAVMVMI
PEAWQNDTHI DPKKKAFYEW AACLMEPWDG PALFTFADGR YCGANLDRNG LRPCRYYVTD
DDRMICASEV GVIEIEPEKI LQKGRLQPGR MLLVDTKEGR IVDDRELKKS VASRFDFKSW
VLANMITMND LTEKLVSREI EVSKEVELST DITVQSDPRL VAFGYSHEQI TFVLAPMAEG
NEALGSMGND NALACISEQP KLLFDYFRQL FAQVTNPPID PIREKIVMSL DCYVGPQGNL
LEMKPDQCNR LLLKSPILST AELINIKHIE KIYPKWSVAI IDTTFEKADG IQGYLNTIDL
VCQAASKAIA DNNQIIILSD RSTSATRVPI SSLIATGAVH HHLVRQKQRS KVALIIETAE
AREVHHACCL VGYGADAINP YLAIETLIRM NKEGLLKKEM SDEEIIKNYK NSVDAGILKV
MSKMGISTLA SYKGAQIFEA LGVDNSVIDR CFAGTASRIK GVTFEYIAQD AFSMHERGYP
NRDTVKPKGL PETGEYHWRD GGDAHINEPV AIASMQDAVR NKNEKAYETY SKKEYEAIKN
CTLRGLLDFD FENSKAVPID QVEPWTEIVR RFFTGAMSYG SISMEAHSTI AVAMNRLGGK
SNTGEGGEDA ARSQINANGD TMRSAIKQIA SGRFGVTSYY LADADELQIK MAQGAKPGEG
GELPGHKVSA EIGKTRHSTP GVGLISPPPH HDIYSIEDLK QLLYDLKCSN PRARTSVKLV
SEVGVGIVAA GVAKAGSENI LVSGGDGGTG AAKLTSIKYA GLPWELGLAE SHQTLVLNDL
RGRVVLQTDG QIRTGRDIAV AALLGAEEWG FATTPLIAMG CIMMRKCLAS DTLVRTTQGL
KKVKDVSVGE YLYGADNTPV LCIGANAPET GSLKEIVYED FDSKKLVSFK CTPDHHLELV
LANAAPELSG STVTWFSSCT GEHKKQDSTF DLESIVSSFY NDLVDSDDII TFDNVCEAID
VALDEHYHRG GSDRYSEKFN GFITQIANEE LKSNPEFVRN ALHEAAEKFM VEDAPKNFAV
TSVSVETTSV ESQSVCKSSC ACGGVRKIVH QFETIEEAEM AYSLLLSDVY DRVDPSFVSN
GYKFQASVEA LEQMCSKDIL HNHLHMYRAP AEQVEPLTHS SSLPVDPYFL GLWLGEGSSD
SATISTTDRE VVVWLQQYVE RLNKDKPAEA SPLRLTKING FKPGQQMANG FVQKVTVPTY
TITSGESFTG GNWNPVYNSL KSMGLLSNKS NGIPEAYKAA DLQSRLALLA GLVDSDGCYV
ESYNSYRFMQ KSELHKKIVY DLKEMATSCG IETTDIDVSE SRLYLGSSET TSAYVVYLGS
GSEKLQQSLL LPRKKMVRIE SCIQESTPFK VQDVANGEFR AIEVSGGKFQ LDNGLQIANC
HLNTCPVGIA TQDPDLRKKF EGTPEHVINF FYYLANELRN IMAQLGFRTI NEMVGRAEKL
KVREDLRNTK NANIDLSPIL TPAHTIRPGV ATHCVRKQDH KLHVRIDNKL IDESEMTLAK
GLPVTIDCDV VNTDRTLGTT LSYRVSKTFG EQGLPHDTIH VNAKGSAGQS FGAFLASGIT
LELEGDANDY IGKGLSGGRI IVYPPRESKF NAEDQIIAGN TAFFGATSGT AFIRGIAAER
FAVRNSGANI VTEGTGDHGC EYMSGGRVVV LGSTGRNFAA GMCGGIAYVL DMAQDFGDKV
NTQTVELSSV TDPAEIAFLR GLIEDHRHYT ESEVADRILN DFNRILPRFV KVLPFDYKKV
LEKEKQKAEE AKKNELSTFL KSIKEDPEAD VTNGEAAKIK KGHVHRPSKA SEPPVLDVED
TVTDSAAAKK PVVKLDKVRG FMKYKRRNEK YRPATERSKD WKEMSSRLTK DELKHETARC
MDCGVPFCTS DTGCPISNVI PKWNELVFQD RWYDAWQRLM MTNNFPEFTG RICPAPCNGA
CVLGINEVPV NIKSIECAII DHAFEQGWVK PEPPAQRTGK TVAVIGSGPA GLAAADQLNK
AGHLVTVFER SDRAGGLMMY GIPNMKLDKR LVKRRTDLMA AEGVEYRCNT TVGEDISMEE
LKSTYDAVVF AVGSTIPRDL KIPGRELTNI KFAMELLHSN TKALLDDNLE EIRKTLAGKH
VVVIGGGDTG NDCLGTSTRH GAKSVTNFEL LPTPPATRPK DNPWPQWPRI FRVDYGHTEV
ATHYGKDPRE YSILSKEFVD DGEGNVKGIK TVRVEWKRSD SGAWQMAEVP GSEEFFPADV
VLLSMGFVGP DADKLEVNKT KRGTIGTLDP NGYKVGANDN VFAAGDCRRG QSLVVWGIQE
GRQCAREVDN YLMGSTRLPG NGSIEQRNYK LLEEYAEKV
//
