ID A4AVP1_MARSH Unreviewed; 392 AA.
AC A4AVP1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|ARBA:ARBA00020367};
DE EC=6.3.3.1 {ECO:0000256|ARBA:ARBA00013047};
DE AltName: Full=AIR synthase {ECO:0000256|ARBA:ARBA00032931};
DE AltName: Full=AIRS {ECO:0000256|ARBA:ARBA00033093};
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000256|ARBA:ARBA00031908};
GN OrderedLocusNames=FB2170_01317 {ECO:0000313|EMBL:EAQ99971.1};
OS Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=313603 {ECO:0000313|EMBL:EAQ99971.1, ECO:0000313|Proteomes:UP000001602};
RN [1] {ECO:0000313|EMBL:EAQ99971.1, ECO:0000313|Proteomes:UP000001602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX PubMed=21037013; DOI=10.1128/JB.01207-10;
RA Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA Cho J.C.;
RT "Complete genome sequence of strain HTCC2170, a novel member of the genus
RT Maribacter in the family Flavobacteriaceae.";
RL J. Bacteriol. 193:303-304(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP
CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981,
CC ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023392};
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 2/2.
CC {ECO:0000256|ARBA:ARBA00004686}.
CC -!- SIMILARITY: Belongs to the AIR synthase family.
CC {ECO:0000256|ARBA:ARBA00010280}.
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DR EMBL; CP002157; EAQ99971.1; -; Genomic_DNA.
DR RefSeq; WP_013304957.1; NC_014472.1.
DR AlphaFoldDB; A4AVP1; -.
DR STRING; 313603.FB2170_01317; -.
DR KEGG; fbc:FB2170_01317; -.
DR eggNOG; COG0150; Bacteria.
DR HOGENOM; CLU_719355_0_0_10; -.
DR OrthoDB; 9802507at2; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000001602; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR004733; PurM_cligase.
DR PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1.
DR PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EAQ99971.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001602}.
FT DOMAIN 48..168
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 182..383
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 392 AA; 43142 MW; 2A62803D81A78E75 CRC64;
MSSSNSERYN QRGVSASKED VHNAIKNIDK GLFPKAFCKI VPDYLTNDDE FCLVMHADGA
GTKSSLAYMY WKETGDISVW KGIAQDALIM NIDDLICVGA TDNIMLSSTI GRNKNLIPGE
VISAIINGTE ELIADLAKHG MVIHSTGGET ADVGDLVRTI IVDSTVTARL KRKEVIDNAN
IKAGDVIVGL ESFGQAIYEK EYNGGMGSNG LTSARHDVFS KYLAEKYPES YDAAVPEDLV
YSGNVKLTEH VSDSPIDAGK LVLSPTRTYA PIVKKMLSKY TSTNIHGMVH CSGGAQTKIL
HFVENLHIIK DNLFPIPPLF KLIQEQSGTD WREMYQVFNC GHRLEIYTNE TVAQDLIEIS
KSFDVDARIV GRVEDGPEKK LTINSEFGSF VY
//
