ID A0A0L8G526_OCTBM Unreviewed; 1098 AA.
AC A0A0L8G526;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=phosphoribosylformylglycinamidine synthase {ECO:0000256|ARBA:ARBA00012747};
DE EC=6.3.5.3 {ECO:0000256|ARBA:ARBA00012747};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000256|ARBA:ARBA00032632};
DE AltName: Full=Formylglycinamide ribotide amidotransferase {ECO:0000256|ARBA:ARBA00029823};
GN ORFNames=OCBIM_22000003mg {ECO:0000313|EMBL:KOF72127.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF72127.1};
RN [1] {ECO:0000313|EMBL:KOF72127.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF72127.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF72127.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004920}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000256|ARBA:ARBA00008608}.
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DR EMBL; KQ423819; KOF72127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L8G526; -.
DR EnsemblMetazoa; Ocbimv22000004m; Ocbimv22000004m.p; Ocbimv22000003m.g.
DR UniPathway; UPA00074; UER00128.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01740; GATase1_FGAR_AT; 1.
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; IPR010073; PurL_large.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR NCBIfam; TIGR01735; FGAM_synt; 1.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF02769; AIRS_C; 2.
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 3: Inferred from homology;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605}.
FT DOMAIN 208..364
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 622..753
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 921
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1057
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1059
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1098 AA; 120088 MW; 5AA221C2B935C6F1 CRC64;
MILDGEIQTK SLFRMVMDTQ DFSNNNSVIK FSDNSSAIDG FEVSVLLPED SSKASPFVVK
EKQKRHIIFT AETHNFPTGV APFPGATTGT GGRIRDVHCT GRGAHVVAGT AGYSFGNLNI
PGYVQPWEEE KKFDGPVKFA SAVDVAIEAS NGASDYGNKF GEPVLAGFAR SFGLCLPNGE
WKEYVKPIMF SAGIGMLEDM HIKKQVAEEG MEVVKIGGPV YRIGVGGGAA SSVEVQGDNK
SDLDFNAVQR GDAEMEQKLN RLIRSCIELK EGNPILSIHD QGAGGNGNVL KELVEPAGAE
IFADNFILAD PTISALELWG AEYQESNALL LMPKDHQLLE KISQRERCPV SFVGRVTGDG
KIKLNGFSST SDGCSDPKRF KDILPVNLDL KHVLGSMPQK NFKLDHLTLD LKPLSIPVEL
TLRESLERVL RLPAVASKRY LTNKVDRSVT GLVAQQQCVG YLHTPLSDVA VTALSYFDTV
GSATAIGEQP IKGLVNPCCG ARMSVGESLT NLIFASVTAL KDVKCSSNWM WAAKLAGEGA
ALYDACKSMC DIMKQLGIAV DGGKDSLSMA ARVGSQTIKA PGTLVVSTYV GCPDIRLSLT
PDLKCSQGRG ILLHVDPSCG QHRIGGSALA QCFKQLGKDV PDLERPDIFK SMFDVTQQCI
SDKLISSGHD ISDGGLITCA LEMAFAGNCS MHLHFENTAN DPPLELLFAE ELGLILELRD
DNQQMVISRY KEAGVPCSII GYCSEENVPQ VTVSVSNQEL LNMKLADLRD IWEETSYQLE
KRQTTIACTE AERKSFRLRK EPPYTFNYDL SQLYNPHSFI LPQHSPSIAI IREEGSNGDR
EMAAAFHYVG FQTWDVNMQD LCSGNITLDQ FRGIAFAGGF SYADVCGSAK GWAATAMFNK
NVKEEFKKFF DRDDTFSFGV CNGCQLMSLL GWVAPYQDDS ITTDHSVTSG GLFLDANDSE
RFESRFVTAK VSESPAIMFE GMAGTVFGIW VSHGEGKMQF KSDSLYRNLK DKHLIPLHYV
NDDGIPTSEY PFNPNGSPDG VAAVCSENGR HVAIMPHPER CFLAWQCPWL PLNMCDDLQV
TPWLKLFANA YNWCKTIQ
//
