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Database: UniProt
Entry: A0A024G4P1_9STRA
LinkDB: A0A024G4P1_9STRA
Original site: A0A024G4P1_9STRA 
ID   A0A024G4P1_9STRA        Unreviewed;      2265 AA.
AC   A0A024G4P1;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=glutamine--fructose-6-phosphate transaminase (isomerizing) {ECO:0000256|ARBA:ARBA00012916};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN   ORFNames=BN9_025980 {ECO:0000313|EMBL:CCI41814.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI41814.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI41814.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI41814.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001031};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCI41814.1}.
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DR   EMBL; CAIX01000025; CCI41814.1; -; Genomic_DNA.
DR   STRING; 65357.A0A024G4P1; -.
DR   InParanoid; A0A024G4P1; -.
DR   OrthoDB; 1705390at2759; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-EC.
DR   GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd06558; crotonase-like; 1.
DR   CDD; cd00714; GFAT; 1.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR045004; ECH_dom.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR005855; GFAT.
DR   InterPro; IPR047084; GFAT_N.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR021133; HEAT_type_2.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   NCBIfam; TIGR01135; glmS; 1.
DR   PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR   PANTHER; PTHR10937:SF0; GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING); 1.
DR   Pfam; PF16113; ECH_2; 1.
DR   Pfam; PF13522; GATase_6; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 5.
DR   PROSITE; PS51464; SIS; 2.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053237};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          127..357
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          432..573
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          606..752
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   REPEAT          1895..1933
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   REPEAT          1934..1972
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   REPEAT          1973..2011
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   REPEAT          2012..2050
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   REPEAT          2088..2126
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
SQ   SEQUENCE   2265 AA;  250648 MW;  6B7BE524E72AE5C4 CRC64;
     MLLHGKKNSG ATLQGLNFHA LLGKSTDMIR QFSRRSPTRL VFDIKAIPLH YSLVYESSIL
     HHRRHIETSY GTIAKVGAKT TTTSVTKTHH AIIGLLLAAG ISLQYGDRKK NGEEYEVSLF
     GKIAECCGIM GVVGKSGNAS NFLLEGVTIL QNRGYDSAGM STQKSIPDEN GQAPITTTKF
     ASVDGTADSI QLLKNSKEQH DGNNVGIAHT RWATHGSKTD HNAHPHMDMH GRVSVIHNGT
     FTNYNEIKQE LTSEGVIFAS DTDTEVAAQL IGHLMGDGAD VLTATRLALS RLEGTWGLCI
     MARDEPGKII VARNGSPLCI GYGSNEMYVA SETTAFSRYT KRFISLKDGE LAVLKSDSAE
     LDPVDEKEGF LQRFPTSRYA TAPDVKVRLA PTPYPHWTIR EIMEQPKAVA AALGYGGRVS
     VDHVYLGGLE AEKERMLKIK NLLIAACGTS LYASKYGAKL MRSLNAFDNV SAEDASECTP
     DRLPRKKAGV LVVSQSGETL DAVRVLKMVE DLPVEFPTFS VVNAVGSLIA RTTKCGVYLN
     AGRENAVAST KAFVTQVTVM GLIACWFAQN RPEGNHTKMD ELIQSMHRLP IAIGIALRTR
     QQCEQVAEKL MSSEHLFVLG RGYGEPIAYE GALKIKELSY LHAEGYPGGA LKHGPFALIE
     DAKDGKNGAT PIILIVLDDE HAQYMKTAAQ EVRARGAHTI VITDNAKMCE GIADTIISIP
     TNGPMTALLA SVPLQLIAYT LAVKKGINPD VPRNLAKAQD AGLRIVKLNR PEALNALSFP
     MIDHLYGRFK KFEKNWTINA VILSGMGERA FCAGGDIRAL YEQGKNEATR HLGKNFFRRE
     YELNYFLATT EMPIISFLNG ITMGGGAGIS MHGKFVVATE KTVFAMPETA IGFFPDVGSS
     YLLPRLGRRL VEGEHYRADV GKSAAMEGQG LGTFLALTGE RLKGPEVIGF GLATHYMESN
     VYDNLMHHLT GFDFPNDMPQ EERDEALHEA LEEFETEDAQ QDIDSEYLQT VESIFGAKNS
     DDTMEGIFSR LKSHNSEWSK TTLATLQKMS PLSLKVTLEL MREGAQKSCE DCFQMEYRIA
     SRMLTKSDMM EGIRSMIIDK DRNPKWTHGS VDDVKREDVL GYFNALENEE ELVLGVSADE
     NANISKDDPV SNTDVSEKLN AKSSALVHSE CTARTEKHVY VPADEDTVSI ITPTSKEHSF
     RISRNLTFQQ LLIDAASYWS LPTSQVVLRD GKGGIWPHSE SVMVTLAAKR NRKIKVILDI
     RQTSWASTFA HLEEACNSKR DQIEPFPKSL PISNASSTLY KDLWGIFTFY CVQGGDLQVD
     LMKAHQFTKL LQDCQLLNKV VKLEIMSIIY NGEINGKVQL NFEEFLNLIS RIAKLAITKK
     LKCIQGCKKE EEAVYQLVVD HILPKACRWP QEEWEVSTIK IHQREVIVFF FGHLKALLAI
     FIFYARSYHK NPATGMREFY MSYQNFQRFI NDFLFAKLQL STVSCAQIFL AACCSCPFHV
     PIYHTVDKDT KVLDPESSSI KAFVATKDVE ETRIATIRDL ISTSGVVVAY TFPASLENRA
     TCMGFSAFID FLGRASLTAY TKSDTISCVK ALIHHVCSEA THARVMEIIE NHGSSCVHAN
     TFYMGTAALK SKFFKAWKEE GFPDYLAANV DVARRPERAV HRKARLLHQR AAMGKNLAIS
     SFQYDSAVSI KASGSVEEEE IHPLKLLMED MSSDEPETRI KSMRKLKTVA QALGHDRTRC
     ELIPFLRDST DNDDEILVAL AEEVGDFVDL VGGPAHAAIL VDPLEVLAGI EETVVRDRAV
     QSLQKVIKAV PNVGEVMVPL LRRLVEGDWF TSRVSACSLF APIYSRLVDV GQKKQVRELF
     SVACSDETPM VRRAAASNIG KVAANVEQEF VVTLIVQLFK TLTSDDQDSV RLLAIENCAA
     IAELLSPEEN QQHILPVVKT SAEDRSWRVR YSIAKDLFPL SRAMGSQITE SELLHCFTTL
     LQDTEAEVRA ASAKNIPGYI TIVKYDLFNN EVIPLLSNLA QDTAPNVRTA VSISCMELAP
     KLGEAAAKTS LSPMLLLFLR DEVVDVRLNI LKRMENLAPW MSSFEDVFLP AIADLARDLQ
     WRVREAVVLS IPSLVGSLGT QYFQEHLLDI YLNAYSDMVG EVRLSATKIL PQLVNTAGNE
     FMLQHVLPRL TAILEKSIIY QERVNVLHAL EQLASESASG ELLNGSITLA IRGAQDKIPN
     VRFVASKTLK ELSKHTDATV IATQVRPCLM ELLNDADTDV NIILQ
//
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