ID A0A085BCU9_9FLAO Unreviewed; 1229 AA.
AC A0A085BCU9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:KFC20294.1};
GN ORFNames=IO90_14035 {ECO:0000313|EMBL:KFC20294.1};
OS Chryseobacterium sp. FH1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1233951 {ECO:0000313|EMBL:KFC20294.1, ECO:0000313|Proteomes:UP000028641};
RN [1] {ECO:0000313|EMBL:KFC20294.1, ECO:0000313|Proteomes:UP000028641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FH1 {ECO:0000313|EMBL:KFC20294.1,
RC ECO:0000313|Proteomes:UP000028641};
RA Pipes S.E., Stropko S.J.;
RT "Epilithonimonas sp. FH1 Genome.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFC20294.1}.
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; JPLZ01000006; KFC20294.1; -; Genomic_DNA.
DR RefSeq; WP_034967482.1; NZ_JPLZ01000006.1.
DR AlphaFoldDB; A0A085BCU9; -.
DR STRING; 1233951.IO90_14035; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR OrthoDB; 9804441at2; -.
DR Proteomes; UP000028641; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02203; PurL_repeat1; 1.
DR CDD; cd02204; PurL_repeat2; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR010141; FGAM_synthase.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR NCBIfam; TIGR01857; FGAM-synthase; 1.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000028641}.
FT DOMAIN 171..218
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 428..581
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 443..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1071
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1202
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1229 AA; 136354 MW; 8F039FD6D0566998 CRC64;
MNKRIFVEKR GIFDVESPKI FDEVKAVVPS IQSVKVYNVY DIFGLNDGEF EKVVNSTFVD
PVTDILVEEN PAEGVYFALE FLPGQYDQRA DSAQQCIALL TGNEKSKVRS GKLIEFEGTS
ESDLTKIKDL LINKVESQEK DLTILNIPSE EAPSKVLVHE NFINFDDAQL EEFFKTHGFA
LGLDDLKFIQ VYFKSEQRNP TETELKVLDT YWSDHCRHTT FETELSNIEF EGQFKHTLET
IFNDYIEKRR FLGRELKPIS LMDLATVCGR YFHKTGQLEN LVVSDEINAC TIQIEAEYDG
KKEPWYLLFK NETHNHPTEI EPFGGASTCL GGAIRDPLSG RSFVFQAMRL TGAADVLESV
DKTLSGKLPQ KTITKQAANG YSSYGNQIGL ATTMVSEIYD EGYKAKRMEV GFVAGAVPVD
WVRREKPEAG DSIIILGGAT GRDGVGGASG SSKEQDETSI HTMSSEVQKG NAVEERKIQR
LFRNPEVTRL IKKSNDFGAG GVSVAIGEIA DSLEVNLDVL PLKYEGLNGT ELAISESQER
MAVVVEPKDK KQFIKFCEAE NIVAVEVAKV TDSGRMQMFW KGDKIVDLSR EFLDTNGCSK
SQEVKITHLN EVKEETPVFN EENFLKILAD KNVASQKGLL EMFDSSIGAT TVAMPLGGKY
QQTLMEGSAQ TLPILGAKDI ETVSFASWGF DAEISKQNSL LGASYAVVES VAKIVAMGCD
YKNIRFSFQE YFEKLGQNPE KWGKPLASLL GAYDAQINFG LAAIGGKDSM SGTYQDLNVP
PTLISFACAN GEKKNVISPE FKQAGNKLYF FNHIPQENGL PNYENMKTVF ELIFENIKAG
KIVSVKTVKE GGVAVALAKM SFGNRLGAEI TVDEKLLLTK NVGSLIIESK EELSTAKLQF
IGEITDFSIL KINDCEFAIE KLLSANTNTF ENLFSTVEKE KITVEIEDKL NSLNPRNIII
KKHGIAQPRV FAPVFPGTNC EYDTLNAFQK EGAIVSSLPL ININHQLLDE SIDAWVKEIK
QSQILAFSGG FSAGDEPDGS AKFIVNVLKN EKMRNAVHEL LDRDGMIIGI CNGFQALVKS
GLLPYGRIKD LDENSPTLAH NAIRRHISQM VNVKVLNDES PWLKGMKDQV FTIPISHGEG
RFMASEAEIQ KLFENGQIAT QYLDLDGNVA HGMPFNPNNS LFGIEGITSP CGKIYGRMGH
PERFAEGLMK NIPTANYHNI FKNGVEYFK
//
