ID B8FNZ8_DESHD Unreviewed; 1284 AA.
AC B8FNZ8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:ACL19523.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:ACL19523.1};
GN OrderedLocusNames=Dhaf_1471 {ECO:0000313|EMBL:ACL19523.1};
OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564 {ECO:0000313|EMBL:ACL19523.1, ECO:0000313|Proteomes:UP000007726};
RN [1] {ECO:0000313|EMBL:ACL19523.1, ECO:0000313|Proteomes:UP000007726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10664 / DCB-2 {ECO:0000313|Proteomes:UP000007726};
RX PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA Tiedje J.M.;
RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT anaerobe capable of dehalogenation and metal reduction.";
RL BMC Microbiol. 12:21-21(2012).
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; CP001336; ACL19523.1; -; Genomic_DNA.
DR RefSeq; WP_015943456.1; NC_011830.1.
DR MEROPS; C56.972; -.
DR KEGG; dhd:Dhaf_1471; -.
DR HOGENOM; CLU_003100_2_0_9; -.
DR Proteomes; UP000007726; Chromosome.
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; 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 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 Ligase {ECO:0000313|EMBL:ACL19523.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 182..231
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 445..597
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 634..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1124
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1256
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1284 AA; 140537 MW; C73B977E74880BB8 CRC64;
MELQSVKRIY VEKKPGFNIE AQGLLQDIQE NLGIKNLEDL RIINRYDVAG ITSEEYAQAR
RIIFSEPTVD WVYDEELKLA PQDRVFAMEY LPGQYDQRAD SARQCIQILT QKERPEIAAA
KVMVLKGQIT EAELERIKQY CINPVESREA GLEKPENLAF VPELPEDVET IEGFTGMAQT
ELEQFYQGAG LAMSLEDLAF CQGYFRDEEK RDPTITEIRV IDTYWSDHCR HTTFFTQLQN
IVIAEGEFAE PIRKAYEEYQ ESRGLVYGEK AESRDVCLMD LAVIGMKELK KKGLLQDLDE
SDEINACSIV VNVDVDGRSE EWLVMFKNET HNHPTEIEPF GGAATCLGGA IRDPLSGRTY
VYQAMRVTGS GDPRAKVEET LPGKLPQRKI TTVAAAGYSS YGNQIGLATG QVAEVYDEGF
IAKRMEIGAV IAAAPRENVV REAPKPGDVV VLVGGRTGRD GCGGATGSSK EHTTESLATC
GAEVQKGNPP TERKIQRLFR NPKVSRMIKK CNDFGAGGVS VAIGELTDGL EIDLDVVPKK
YEGLDGTELA ISESQERMAV VIAAENLEAF VGYADEENLE ATLVAKVSEH PRLNMTWRGQ
TIVDISREFL NTNGVKQKTD VSVLLPESSE NYFRQLPQGG RSGETASGAA ADSSSGAAAG
DMSLAGMALE DAWLANLQDL NVCSQKGLVE RFDSTIGANT VLMPFGGKYQ ATPAEGMVAK
IPVESGDTRT ATAMTYGYNP QCAQWSPFHG ALYAVVEAVT KMVALGADYR SIHLTLQEYF
EKLGKDPQKW GKPFSALLGA FYAQKKLGIP AIGGKDSMSG TFMDLHVPPT LVAFAVGVLN
TDRVISQEFK QAGSQVVLVP AKRDRDEVID FEHLAGNYDK VHELIHGGKV LSSHTVKMGG
LAAALTKMAF GNRIGMKFSS PMAGADLFRA DYGSIILEIP AAVELRDALG EVRYMVLGST
QEKPAIELNE AEIFLDKALA IWEKPLERIF PTKTATVDQP QKISFSERNS QRPAIKLAKP
RVFIPVFPGT NCEYDSERAF TKAGAVVETL VIRNLTPDHV EESIAGIVKG IERAQMVMLP
GGFSAGDEPD GSGKFIATMF RNPRIKEAVM KLLKQRDGLM LGICNGFQAL IKLGLVPYGE
IMDLDEEAPT LTYNKIGRHV SCMVQTKVVS TLSPWFSGME LGDIHTIPVS HGEGRFVASP
DVVRKLMERG QVATQYVDHQ GCPSNEVLYN PNGSYEAIEG ITSPDGRVLG KMGHSERVGE
GVAINISGNK YQPIFAGGVN YFRG
//
