ID H5Y3Q1_9FIRM Unreviewed; 1275 AA.
AC H5Y3Q1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase, clade II {ECO:0000313|EMBL:EHQ89295.1};
GN ORFNames=DesyoDRAFT_2210 {ECO:0000313|EMBL:EHQ89295.1};
OS Desulfosporosinus youngiae DSM 17734.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=768710 {ECO:0000313|EMBL:EHQ89295.1, ECO:0000313|Proteomes:UP000005104};
RN [1] {ECO:0000313|EMBL:EHQ89295.1, ECO:0000313|Proteomes:UP000005104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17734 {ECO:0000313|EMBL:EHQ89295.1,
RC ECO:0000313|Proteomes:UP000005104};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Land M.L., Hauser L., Pester M.,
RA Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.,
RA Woyke T.J.;
RT "The Noncontiguous Finished genome of Desulfosporosinus youngiae DSM
RT 17734.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CM001441; EHQ89295.1; -; Genomic_DNA.
DR RefSeq; WP_007782870.1; NZ_CM001441.1.
DR AlphaFoldDB; H5Y3Q1; -.
DR STRING; 768710.DesyoDRAFT_2210; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_003100_2_0_9; -.
DR OrthoDB; 9804441at2; -.
DR Proteomes; UP000005104; 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; 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:UP000005104}.
FT DOMAIN 185..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 ACT_SITE 1115
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1275 AA; 139907 MW; ECD7C080D1440A46 CRC64;
MESQAVKRIY VEKKPGYDIE AQGLYTDLIE NLGILGLQGL RVINRYDISG ITDEEYAKSR
PIIFAEPPLD LVYDEELDIP AQDRVFAMEY LPGQYDQRAD SAAQCVQILT QKERPAIASA
KLIVLKGEIS EDDFQRIKEY CINPVESREA ALEKPESLEF EAVIPPDVEI LDRFMEKSPA
ELREFFKETG LAMSYEDLAF CQTYFRDTEK RNPTITEIRV IDTYWSDHCR HTTFNTKIEE
VSFSEGEFSF PINTAYQEYL TSRDYVYGEN SAHRDVCLMD IAVLGMKELK KQGKLPDLDL
SDEINACSIV VNADINGQTE EWLVMFKNET HNHPTEIEPF GGAATCLGGA IRDPLSGRTY
VYQAMRVTGS GDPRARLEDT LPGKLPQRKI TTGAAAGYSS YGNQIGLATG QVTEVYDEGF
VAKRMEIGAV IAAAPRENVV REAPQAGDVV VLVGGRTGRD GCGGATGSSK EHTTESLLTC
GAEVQKGNPP TERKIQRLFR NPKVSTLIKR CNDFGAGGVS VAIGELTDGL EINLDAVPKK
YEGLDGTELA ISESQERMAV VIRAEDFETF ADYAHQENLE ATLVAKVSSN PRLIMHWRRQ
AIVDLSREFL DTNGVKQKTR VRVSQPEAKQ NYFSKLPELV AEKITSYNSE NNPENRGSLL
KEAWLANLSD LNVCSQKGLV ERFDSTIGMS SVLMPLGGKY QATPAEGMAA KLPVLSGETN
TATMMTYGYN PQLAKWSPFH GALYAVIDAV TKTVALGGDY SQVRLTLQEY FERLGTDPEK
WGKPFSALLG AFYAQKNLGI PAIGGKDSMS GTFMDLNVPP TLVAFAVNVI KADKVVSQEF
KKPGSQVVLV KAERDVHEVP DFEQLSKNYL KVNQLIDSGY VLASHTVRIG GLAAALSKMA
FGNRIGVALE NSLDLQSLFR ADYGSILLEI EESVDLAEVF GGAAYQFLGV TQENPVITVN
GATIELETAL AAWEKPLEKI FPTQTEKVAQ PQTVSFRLRN TLTPSIKVAK PRVFIPVFPG
TNCEYDSAAA FEKAGGIVET LVIRNLSAAD VEQSIQEMVK KINQAQIVML PGGFSAGDEP
DGSGKFIATM FRNPRISEAI AGLMNQRDGL MLGICNGFQA LIKLGLVPYG EIIDLMEDSP
TLTYNKIGRH VSSMVQTKVV SVLSPWFSGV NLGDIHSVPI SHGEGRFVAD PDMIQTLIHN
GQVATQYVDL NGNPSNDVLY TPNGSFEAIE GITSPDGRIL GKMAHSERTG PEIAKNIPGN
KYQPIFAGGV NYFRG
//
