ID G7XUU0_ASPKW Unreviewed; 375 AA.
AC G7XUU0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=D-alanine--D-alanine ligase (D-alanylalanine synthetase) (D-Ala-D-Ala ligase) {ECO:0000313|EMBL:GAA90679.1};
GN ORFNames=AKAW_08793 {ECO:0000313|EMBL:GAA90679.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA90679.1};
RN [1] {ECO:0000313|EMBL:GAA90679.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA90679.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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; DF126475; GAA90679.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XUU0; -.
DR STRING; 1033177.G7XUU0; -.
DR VEuPathDB; FungiDB:AKAW_08793; -.
DR eggNOG; ENOG502QPTY; Eukaryota.
DR InParanoid; G7XUU0; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:GAA90679.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 142..357
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 375 AA; 41071 MW; 4A2C6C7D38D89522 CRC64;
MSLPMTQITR SLHNATTPPV VAVLYQAIEP PIINGARKPR KPGGYQDSGS DIAYTLKNRG
VRVVTPVSSP NPKEQEGWCF PDTENGILSA VRQGATHLWA NTILFSSHPL QASQSLDSAP
ISVVGQPPTL VESFDDKAYL NDRLRIHGSF TLPRSWLIRN SDNISPILDS IPNYPVVGKP
VRGRGSHGVK VCHNRAELEA HLNALLLESP IVMVEEYLTG EEATITVMPP STENPEHWSL
PPITRFNHVD GIAPYNGTVA VTANSRAITE TEMQDESYRS AMRQCEQVAK LIGATAPIRI
DIRRFSEGSQ FAIFDINMKP NMTGPGRPGR EDQASLTALA AAAIGWDYGA LLHKILNSAQ
PLDRFRAYTN PFASH
//
