ID Q8PY18_METMA Unreviewed; 700 AA.
AC Q8PY18;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE SubName: Full=D-alanine-D-alanine ligase related protein {ECO:0000313|EMBL:AAM30744.1};
GN OrderedLocusNames=MM_1048 {ECO:0000313|EMBL:AAM30744.1};
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952 {ECO:0000313|EMBL:AAM30744.1, ECO:0000313|Proteomes:UP000000595};
RN [1] {ECO:0000313|EMBL:AAM30744.1, ECO:0000313|Proteomes:UP000000595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
RC {ECO:0000313|Proteomes:UP000000595};
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baumer S., Jacobi C.,
RA Bruggemann H., Lienard T., Christmann A., Bomeke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.P., Gunsalus R.P.,
RA Fritz H.J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; AE008384; AAM30744.1; -; Genomic_DNA.
DR RefSeq; WP_011032997.1; NC_003901.1.
DR AlphaFoldDB; Q8PY18; -.
DR GeneID; 24837841; -.
DR KEGG; mma:MM_1048; -.
DR PATRIC; fig|192952.21.peg.1227; -.
DR eggNOG; arCOG01791; Archaea.
DR HOGENOM; CLU_430627_0_0_2; -.
DR Proteomes; UP000000595; Chromosome.
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 GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 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 Gene3D; 2.20.25.110; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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 Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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:AAM30744.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 422..634
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 78681 MW; 835E50ADED059DE1 CRC64;
MTQNNIDSNS RRKRAKGAVQ TKTLGPVEDL ETHVRSDWWQ TLFNSLYLKT DADLLDDIEV
TKKEADLVVS ILGLNPEDAV LDLCCGQGRH VLELARRGFP NVEGYDRSQY LIRKARTRAQ
KENLQVRFRE GDARKLPYPS DTFSVVTILG NSFGYFDSTL QDRKVLEEVF RVLKPGGRVF
IDAVDGDHIR KNFQPRSWEW LDRKYFVCRE RALSSDCERL ICREVICRID RGIIADQFYA
ERLYNRESLF ELLTASGFSS PTFHTTFSPV STGTQDAGMM EKRILLSATV EKAWPSMESS
GAESKKPLNV VVVLGDPRKE DQVKPACVFD DDDFETINRM KTALSEIPSI KFTFLDRHET
LFEDLRKKAG KTDLVLNLCD EGFYNDPVKE LHVPAMFEQL NIPYTGAGPQ CLAYCYDKSL
VRGVAREMRI PVAKGVLVTD DSDISRLSLS FPLLVKPNSG DSSFGITQKS IVHSREELLD
IMKETREKIG SDKPLLLEEF LPGKDISVGI IGNPPSCTVL PITEEDYSAV PGELPKICGY
EAKWLPDSSY WKIKSVPADL PEKTQKEVVR SCLALFTRLG CRDYARFDWR LDAEGRPRLL
EVNPNPGWCW DGHLAKMAAY ANISYSGMLA AIIGAAKKRY GIGLGGKVVL QTKAGQSTRK
SPAECAAEFE EEVEAKSSIE PGNGRKRNVF SSNSETIKVL
//
