ID W4E585_9BACL Unreviewed; 408 AA.
AC W4E585;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Amino acid ligase of ATP-grasp superfamily protein {ECO:0000313|EMBL:ETT75112.1};
GN ORFNames=C173_07946 {ECO:0000313|EMBL:ETT75112.1};
OS Paenibacillus sp. FSL R7-277.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1227352 {ECO:0000313|EMBL:ETT75112.1, ECO:0000313|Proteomes:UP000019051};
RN [1] {ECO:0000313|EMBL:ETT75112.1, ECO:0000313|Proteomes:UP000019051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-277 {ECO:0000313|EMBL:ETT75112.1,
RC ECO:0000313|Proteomes:UP000019051};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
CC -!- PATHWAY: Purine metabolism. {ECO:0000256|ARBA:ARBA00025704}.
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:ETT75112.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ASPX01000019; ETT75112.1; -; Genomic_DNA.
DR RefSeq; WP_051477907.1; NZ_ASPX01000019.1.
DR AlphaFoldDB; W4E585; -.
DR PATRIC; fig|1227352.4.peg.1595; -.
DR eggNOG; COG0189; Bacteria.
DR OrthoDB; 2210549at2; -.
DR Proteomes; UP000019051; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR Pfam; PF02222; ATP-grasp; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ETT75112.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 110..300
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 408 AA; 46190 MW; 38CB667797F28750 CRC64;
MAVLILNQRR RAFAPYLTWL EDLDEEVYLY TSPAYGEITE PFALVQVFDN WVSNDRVEID
ALRLYEEHPY RLIIALDESD LIRAARLRER LHLPGQQLES AVAYRDKAVM KSLVSPQVSC
PAFRRLASPL HLYDFVLEHG LPVVVKPVDG MGSMNTDIIR TREQLNDVWE RGLGSGLMVE
AYVEGEMYEI DGLMMGQEIR FASVGKYSCK PLEILQQDCF VELLSPGCAV YERLVHEVQQ
VIEALPSPGV STFHCEMFHT PEDEWVFCEI ASRTAGGRIS ESISAMYDVD LNREWVRGQC
GLPLKLPVPR PSQVAGVYLM PKRPGTVKTI PQTLPFEWVK EYVPRVKEGE QLDAAHSSVD
AVMTVIIVGE NSASLQVRLS QLLRYLEQEV QILPAYKEDT TNEAPVTS
//
