ID C4LH52_CORK4 Unreviewed; 862 AA.
AC C4LH52;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000256|HAMAP-Rule:MF_00420};
DE Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00420};
DE EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00420};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000256|HAMAP-Rule:MF_00420};
DE Short=FGAR amidotransferase II {ECO:0000256|HAMAP-Rule:MF_00420};
DE Short=FGAR-AT II {ECO:0000256|HAMAP-Rule:MF_00420};
DE AltName: Full=Glutamine amidotransferase PurL {ECO:0000256|HAMAP-Rule:MF_00420};
DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000256|HAMAP-Rule:MF_00420};
GN Name=purL {ECO:0000256|HAMAP-Rule:MF_00420};
GN OrderedLocusNames=ckrop_0378 {ECO:0000313|EMBL:ACR17157.1};
OS Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS CCUG 35717).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR17157.1, ECO:0000313|Proteomes:UP000001473};
RN [1] {ECO:0000313|EMBL:ACR17157.1, ECO:0000313|Proteomes:UP000001473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC {ECO:0000313|Proteomes:UP000001473};
RX PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT revealed insights into the physiology of a lipophilic corynebacterium that
RT lacks mycolic acids.";
RL J. Biotechnol. 136:22-30(2008).
CC -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
CC complex involved in the purines biosynthetic pathway. Catalyzes the
CC ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and
CC glutamine to yield formylglycinamidine ribonucleotide (FGAM) and
CC glutamate. The FGAM synthase complex is composed of three subunits.
CC PurQ produces an ammonia molecule by converting glutamine to glutamate.
CC PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-
CC dependent manner. PurS interacts with PurQ and PurL and is thought to
CC assist in the transfer of the ammonia molecule from PurQ to PurL.
CC {ECO:0000256|HAMAP-Rule:MF_00420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00420};
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. {ECO:0000256|HAMAP-
CC Rule:MF_00420}.
CC -!- SUBUNIT: Monomer. Part of the FGAM synthase complex composed of 1 PurL,
CC 1 PurQ and 2 PurS subunits. {ECO:0000256|HAMAP-Rule:MF_00420}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420}.
CC -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000256|HAMAP-
CC Rule:MF_00420}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00420}.
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DR EMBL; CP001620; ACR17157.1; -; Genomic_DNA.
DR RefSeq; WP_012731045.1; NC_012704.1.
DR AlphaFoldDB; C4LH52; -.
DR STRING; 645127.ckrop_0378; -.
DR KEGG; ckp:ckrop_0378; -.
DR eggNOG; COG0046; Bacteria.
DR HOGENOM; CLU_003100_0_1_11; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000001473; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02203; PurL_repeat1; 1.
DR CDD; cd02204; PurL_repeat2; 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 HAMAP; MF_00420; PurL_2; 1.
DR InterPro; IPR010074; PRibForGlyAmidine_synth_PurL.
DR InterPro; IPR041609; PurL_linker.
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 NCBIfam; TIGR01736; FGAM_synth_II; 1.
DR PANTHER; PTHR43555; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 1.
DR PANTHER; PTHR43555:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 1.
DR Pfam; PF00586; AIRS; 2.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00420};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00420, ECO:0000313|EMBL:ACR17157.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00420};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00420}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_00420}; Reference proteome {ECO:0000313|Proteomes:UP000001473}.
FT DOMAIN 67..109
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 135..249
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 263..418
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 507..626
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 672..808
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 105
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 155..158
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 374..376
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 564
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 602
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 604
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
SQ SEQUENCE 862 AA; 91006 MW; 84D847514719BF07 CRC64;
MVNQANKNQT NKTDMNTEDD QMLKSTETAR TDAGADNAAA DNAVESFTAA QVNDTVAAAQ
SDPDASQPYA SLGLKDDEYA RIKDILGRRP TDAELAMYSV MWSEHCSYKS SKVHLRYFGE
TMTKEMSSKI LAGIGENAGV IDIGDGNAVT FRVESHNHPS YVEPHQGAAT GVGGIVRDIM
AMGARPIAVM DQLRFGPADA ADTQRVLPGV IDGVGGYGNC LGLPNIGGET VFDESYAGNP
LVNALCIGTL KVDDLKLAFA SGKGNKVMLF GSRTGLDGIG GVSVLASDTF EDGAERKLPS
VQVGDPFAEK VLIECCLDLY HAGIVVGIQD LGGAGLSCAT SELAAAGDGG MEVNLDAVPL
RAENMTAAEI LSSESQERMC AVVTPENVDR FREICAHWDV TCAEIGEVTD GDHLVIRHHG
QVVVDAPAHT IAHQGPVYDR PYERPDWQDD LQEPGVETKG FARTQGADEL RETWLRMVAS
PALCSRAFIT EQYDRYVMGN TVEAQNADAG VLRIDESTGR GVAVSADASG RYTKLDPNMG
ARLALAEAYR NVVVTGARPV AVTNCLNFGS PEDPAVMWQF REAVHGLADG ARELGIPVSG
GNVSFYNQTG SEAILPTPLV GVAGVVTSVD HHINHLLGGL TTERSAFPES ESDAGDDSSA
STSGSANDQF EELYLLGETH DELGGSIWQQ VKHNALSGLP PQVDLAATSA LADFFCDQAD
PDTPRVVTAA HDLSEGGLAQ ALAELAMISG VGMDVDVSKV HADPCVALFS ESANRVVVAC
AHGDGDKLVS LAKRCGIPVL RLGSVTSRAC GSSQETSAQV RVRVSTDEAD EIMLPVSELR
EAWTSTLPKL FAHAAGANSV VE
//
