ID A0A3N2LZT4_9BACT Unreviewed; 1235 AA.
AC A0A3N2LZT4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:ROT03401.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:ROT03401.1};
GN ORFNames=EEL33_17390 {ECO:0000313|EMBL:ROT03401.1};
OS Muribaculaceae bacterium Isolate-037 (Harlan).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX NCBI_TaxID=2486461 {ECO:0000313|EMBL:ROT03401.1, ECO:0000313|Proteomes:UP000275399};
RN [1] {ECO:0000313|EMBL:ROT03401.1, ECO:0000313|Proteomes:UP000275399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate-037 (Harlan) {ECO:0000313|Proteomes:UP000275399};
RA Clavel T., Strowig T.;
RT "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT host preference, and functional potential of this yet undescribed family.";
RL Submitted (NOV-2018) 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:ROT03401.1}.
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DR EMBL; RIAZ01000029; ROT03401.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2LZT4; -.
DR Proteomes; UP000275399; 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: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.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:ROT03401.1};
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:UP000275399}.
FT DOMAIN 179..222
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 434..584
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 448..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1235 AA; 134789 MW; 00BE343DA2AE9590 CRC64;
MTPYRIFVEK REPYRVEAES LRNELNSNLG LNIRDLRLLC VYDLFGFTPE LVEKSSYKVF
GEPATDNVSK EVDFEGRPYL AIESLPGQFD QRAAAAVECV KLIKPDADIE IRSARLIIFD
ASVGDEEMKK IAHYCINAVE SRQKDLSILA APERAAAKPV PVLEGFREIT ADQAPAWCKE
KGLAMNGDDL MEVVKYFTAE GRDPNETELR ILDTYWSDHC RHTTFTTELT DIKVNDSFAS
ADLEESLRQW HEIRKELGRE HKPLCLMDLA TIGARYLLKT GQLNDLEQSE ENNACSIYVD
VDVDGEKERW LLQFKNETHN HPTEIEPFGG ASTCLGGAIR DPLSGRSYVY QAMRVTGAGD
IYKPVSETME GKLPQRVISL RAAAGYSSYG NQIGLATTHV REIYHPDYVA KRLEVGAVVG
AVKASDVRRE SPAEGDVVLM FGGRTGRDGI GGATGSSKEH TTSSLEECGS EVQKGNAPEE
RKIARLFRRP EVTRLIKKSN DFGAGGVSVA IGELTDGLDI HLDRVPTKYS GLNTTELAIS
ESQERMSVVV EKKDMDEFIK YCHEENLEVN HVADVTSTGR MRMFYGDKVV ADLSREFIDS
AGARHFAEAT IGTIEPRDPF VHEVAGNSLK DKFLNLLADD NVTSQKGLIE HFDSSIGKST
VLMPFGGKTQ GTEAQVSVQK LPVGNHHTDT ASMMAFGFNP YLTSWSPYHG AAYSVVEAIS
KAVAAGADYE RMRFSYQEYF ERMHTRESWG KPLAALLGTL RMQTEFGLAS IGGKDSMSGT
FANISVPPTL IAFGVAPVDS RNVISPEFKA AGNYIYVVRH NPLPSLMPDS EKLKTNYKLL
QRLIEEGTVV SGYALGFGGL TEAIAKMSFG NRIGVNITAK EDDLFNYGNG SIVVESKDIL
NLPDFDLIGE TVAEPTLTVN GEKISIDEAF EANRVRFTAV YPDRTAVSGK VENATSGSEV
AKYKGEPKDN PVVYLPVFPG TNCDYDMAAS FAKEGAVVTT SVFCNQTAED IEKSTSDMAA
HIDACDILAF SGGFSEGDEP DGSGKFIASV IMNEKVKAAI ERLHARGGLI LGICNGFQAL
VKSGLLPFGK IGELTADSPT LFHNDINRHI SQIVNTRVGS VASPWLAGFE LGEMHAVAAS
HGEGKFVANA ELAATLRKNG QIAFQYADSE GNATMDSPAN PNGSTEAIEG IISPDGLILG
KMAHSERYAD GLMKNIAGNK SQNLFANAVA YFKAK
//
