ID T0I0E0_9FIRM Unreviewed; 1262 AA.
AC T0I0E0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase, synthetase subunit {ECO:0000313|EMBL:EQB22460.1};
GN ORFNames=UNSWDHB_207 {ECO:0000313|EMBL:EQB22460.1};
OS Dehalobacter sp. UNSWDHB.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Dehalobacter.
OX NCBI_TaxID=1339256 {ECO:0000313|EMBL:EQB22460.1, ECO:0000313|Proteomes:UP000015814};
RN [1] {ECO:0000313|EMBL:EQB22460.1, ECO:0000313|Proteomes:UP000015814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNSWDHB {ECO:0000313|EMBL:EQB22460.1,
RC ECO:0000313|Proteomes:UP000015814};
RX PubMed=24051315;
RA Deshpande N.P., Wong Y.K., Manefield M., Wilkins M.R., Lee M.;
RT "Genome Sequence of Dehalobacter UNSWDHB, a Chloroform-Dechlorinating
RT Bacterium.";
RL Genome Announc. 1:e00720-13(2013).
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:EQB22460.1}.
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DR EMBL; AUUR01000040; EQB22460.1; -; Genomic_DNA.
DR AlphaFoldDB; T0I0E0; -.
DR PATRIC; fig|1339256.3.peg.381; -.
DR Proteomes; UP000015814; 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}.
FT DOMAIN 185..230
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 444..596
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1103
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1233
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1235
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1262 AA; 138166 MW; 3ED387A321BF0BCC CRC64;
MLQAVKRLFV EKKQGFNIEA QGLFADLRDN LSIAGLQGVR MINRYDISGI TDEEYEKSRT
IIFAEPPLDI LYEETLNISS GDRVFAMEYL PGQYDQRADS AAQCIQMLTQ KERPLIASAK
VIILEGRLSD QDFARIKQYC INPVESREAS LAKPQSLEFE AAEPADVEIM EEFITKTPEE
ITVMQQRMNL AMSVEDLLFC QSNFRNTEKR NPTMTEIKTI DTYWSDHCRH TTFQTEIEEV
DIKDGNFSGP IKTAFDCYKA SRAKVYQDKL PTKDICLMDI ATMGMKELKM AGLLNDLDES
DEINACSIVV TAEVNGREEE WLVMFKNETH NHPTEIEPFG GAATCLGGAI RDPLSGRTYV
YQAMRVTGSG DPRVKVEDTL SGKLPQRKIT TVAAAGYSSY GNQIGLATGQ VAEVYDEGFI
AKRMEIGAVI GAAPRKNVIR KPPEEGDVIV LVGGRTGRDG CGGATGSSKE HTLESLTSCG
AEVQKGNPPN ERKIQRLFRN PEVSTLIKKC NDFGAGGVSV AVGELTDGLD ICLDAVPKKY
ESLDGTELAI SESQERMAVV LAAEDWDKFK SLATEENLEA TVIARVTGDH RLKMSWRGKT
ILDLSRDFLD TNGVKQKTKV EVAAPLETQN YFNAIPSSVA RELPDLRKAW NANLGDLNVC
SKKGLIERFD STIGAASVLM PLGGKYQLSP AEGMVAKLPV LEGDTTTATI MTYGYNPQLA
KWSPFHGALY AVLDAVTKAV ALGGDYHKIR LTLQEYFGKL NDAGKWGQPF SALLGAYYAQ
KQLGIPAIGG KDSMSGSFME LNVPPTLVAF AVCTADARKV VSQEFKQAGS NVVLLKLTRD
EQEIPDFAMA AKNFVKVSDL IQSGWVRSSR SIRMGGIAGA VSEMAFGNMI GFHFSRQIES
SDLFRTDYGS ILLELDEKAD LPALFGDVEY ELLGCTQEKP AIAVNGVELL LTDMLGQWEM
PLEKIFPSKG ENAENTEKPR AVSFDKRSTF RPAIKAAKPR VFIPVFPGTN CEYDSAKAFT
KAGGLVETMV IRNLSAADIE GSIKEMVKII NNSQIIMLPG GFSAGDEPDG SGKFIATLFN
NPRIKDAVMN LLKQRDGLML GICNGFQALI KLGLVPYGEI KEINAEDPTL TYNKIGRHVS
CMARTKVVST LSPWFSGVEL GEIHTIAVSH GEGRFVASQE VISKLIQNGQ IATQYVDLNG
MVSNDIKDNP NGSFEAIEGI TSPDGRVLGK MAHSERTGTG VAVNVPGNKY QSIFEGGIHY
FN
//
