GFA1_CANAL
ID GFA1_CANAL Reviewed; 713 AA.
AC P53704; A0A1D8PJE2; Q5AJV2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing];
DE Short=GFAT;
DE EC=2.6.1.16;
DE AltName: Full=D-fructose-6-phosphate amidotransferase;
DE AltName: Full=Hexosephosphate aminotransferase;
GN Name=GFA1; OrderedLocusNames=CAALFM_C302280CA; ORFNames=CaO19.1618;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061;
RX PubMed=8636033; DOI=10.1128/jb.178.8.2320-2327.1996;
RA Smith R.J., Milewski S., Brown A.J., Gooday G.W.;
RT "Isolation and characterization of the GFA1 gene encoding the
RT glutamine:fructose-6-phosphate amidotransferase of Candida albicans.";
RL J. Bacteriol. 178:2320-2327(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 347-713, AND SUBUNIT.
RX PubMed=17681543; DOI=10.1016/j.jmb.2007.07.002;
RA Raczynska J., Olchowy J., Konariev P.V., Svergun D.I., Milewski S.,
RA Rypniewski W.;
RT "The crystal and solution studies of glucosamine-6-phosphate synthase from
RT Candida albicans.";
RL J. Mol. Biol. 372:672-688(2007).
CC -!- FUNCTION: Involved in amino sugar synthesis (formation of chitin,
CC supplies the amino sugars of asparagine-linked oligosaccharides of
CC glycoproteins).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-
CC fructose 6-phosphate: step 1/1.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17681543}.
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DR EMBL; X94753; CAA64380.1; -; Genomic_DNA.
DR EMBL; CP017625; AOW28265.1; -; Genomic_DNA.
DR PIR; JC6012; JC6012.
DR RefSeq; XP_721697.2; XM_716604.2.
DR PDB; 2POC; X-ray; 1.80 A; A/B/C/D=347-713.
DR PDB; 2PUT; X-ray; 1.90 A; A/B/C/D=347-713.
DR PDB; 2PUV; X-ray; 1.90 A; A/B/C/D=347-713.
DR PDB; 2PUW; X-ray; 3.15 A; A/B=347-713.
DR PDBsum; 2POC; -.
DR PDBsum; 2PUT; -.
DR PDBsum; 2PUV; -.
DR PDBsum; 2PUW; -.
DR AlphaFoldDB; P53704; -.
DR SMR; P53704; -.
DR BioGRID; 1219651; 6.
DR STRING; 237561.P53704; -.
DR BindingDB; P53704; -.
DR PRIDE; P53704; -.
DR GeneID; 3636557; -.
DR KEGG; cal:CAALFM_C302280CA; -.
DR CGD; CAL0000176261; GFA1.
DR VEuPathDB; FungiDB:C3_02280C_A; -.
DR eggNOG; KOG1268; Eukaryota.
DR HOGENOM; CLU_012520_5_2_1; -.
DR InParanoid; P53704; -.
DR OrthoDB; 262871at2759; -.
DR BioCyc; MetaCyc:MON-13172; -.
DR BRENDA; 2.6.1.16; 1096.
DR UniPathway; UPA00113; UER00528.
DR EvolutionaryTrace; P53704; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IDA:CGD.
DR GO; GO:0006038; P:cell wall chitin biosynthetic process; IMP:CGD.
DR GO; GO:0006031; P:chitin biosynthetic process; IMP:CGD.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IBA:GO_Central.
DR GO; GO:0006042; P:glucosamine biosynthetic process; IDA:CGD.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IGI:CGD.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Glutamine amidotransferase;
KW Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..713
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing]"
FT /id="PRO_0000135287"
FT DOMAIN 2..316
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 389..528
FT /note="SIS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 561..703
FT /note="SIS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT CONFLICT 16
FT /note="K -> R (in Ref. 1; CAA64380)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="I -> V (in Ref. 1; CAA64380)"
FT /evidence="ECO:0000305"
FT HELIX 354..360
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 362..370
FT /evidence="ECO:0007829|PDB:2POC"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:2POC"
FT TURN 376..379
FT /evidence="ECO:0007829|PDB:2POC"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 390..394
FT /evidence="ECO:0007829|PDB:2POC"
FT STRAND 396..403
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 405..422
FT /evidence="ECO:0007829|PDB:2POC"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 431..436
FT /evidence="ECO:0007829|PDB:2POC"
FT STRAND 445..454
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 457..468
FT /evidence="ECO:0007829|PDB:2POC"
FT STRAND 472..479
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 483..487
FT /evidence="ECO:0007829|PDB:2POC"
FT STRAND 488..493
FT /evidence="ECO:0007829|PDB:2POC"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 506..522
FT /evidence="ECO:0007829|PDB:2POC"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:2POC"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:2PUW"
FT HELIX 530..550
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 551..553
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 554..562
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 564..567
FT /evidence="ECO:0007829|PDB:2POC"
FT STRAND 569..575
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 580..594
FT /evidence="ECO:0007829|PDB:2POC"
FT STRAND 597..602
FT /evidence="ECO:0007829|PDB:2POC"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:2POC"
FT STRAND 620..623
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 631..642
FT /evidence="ECO:0007829|PDB:2POC"
FT STRAND 648..652
FT /evidence="ECO:0007829|PDB:2POC"
FT STRAND 665..669
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 674..676
FT /evidence="ECO:0007829|PDB:2POC"
FT HELIX 677..695
FT /evidence="ECO:0007829|PDB:2POC"
SQ SEQUENCE 713 AA; 79254 MW; 390C6B8AE756C5E2 CRC64;
MCGIFGYVNF LVDKSKGEII DNLIEGLQRL EYRGYDSAGI AVDGKLTKDP SNGDEEYMDS
IIIKTTGKVK VLKQKIIDDQ IDRSAIFDNH VGIAHTRWAT HGQPKTENCH PHKSDPKGEF
IVVHNGIITN YAALRKYLLS KGHVFESETD TECIAKLFKH FYDLNVKAGV FPDLNELTKQ
VLHELEGSYG LLVKSYHYPG EVCGTRKGSP LLVGVKTDKK LKVDFVDVEF EAQQQHRPQQ
PQINHNGATS AAELGFIPVA PGEQNLRTSQ SRAFLSEDDL PMPVEFFLSS DPASVVQHTK
KVLFLEDDDI AHIYDGELRI HRASTKSAGE STVRPIQTLE MELNEIMKGP YKHFMQKEIF
EQPDSAFNTM RGRIDFENCV VTLGGLKSWL STIRRCRRII MIACGTSYHS CLATRSIFEE
LTEIPVSVEL ASDFLDRRSP VFRDDTCVFV SQSGETADSI LALQYCLERG ALTVGIVNSV
GSSMSRQTHC GVHINAGPEI GVASTKAYTS QYIALVMFAL SLSNDSISRK GRHEEIIKGL
QKIPEQIKQV LKLENKIKDL CNSSLNDQKS LLLLGRGYQF ATALEGALKI KEISYMHSEG
VLAGELKHGI LALVDEDLPI IAFATRDSLF PKVMSAIEQV TARDGRPIVI CNEGDAIISN
DKVHTTLEVP ETVDCLQGLL NVIPLQLISY WLAVNRGIDV DFPRNLAKSV TVE
