ID K6YN30_9ALTE Unreviewed; 334 AA.
AC K6YN30;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:GAC19592.1};
GN ORFNames=GARC_2626 {ECO:0000313|EMBL:GAC19592.1};
OS Paraglaciecola arctica BSs20135.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC19592.1, ECO:0000313|Proteomes:UP000006327};
RN [1] {ECO:0000313|EMBL:GAC19592.1, ECO:0000313|Proteomes:UP000006327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSs20135 {ECO:0000313|EMBL:GAC19592.1,
RC ECO:0000313|Proteomes:UP000006327};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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:GAC19592.1}.
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DR EMBL; BAEO01000034; GAC19592.1; -; Genomic_DNA.
DR RefSeq; WP_007620610.1; NZ_BAEO01000034.1.
DR AlphaFoldDB; K6YN30; -.
DR STRING; 493475.GARC_2626; -.
DR eggNOG; COG1181; Bacteria.
DR Proteomes; UP000006327; 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:GAC19592.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000006327}.
FT DOMAIN 106..302
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 334 AA; 37435 MW; 056C36C317FA6986 CRC64;
MNIEVITTSD KTFRKTGFGS LSSCNDVVES IQRAGNAARL TVCASLDDLQ AVVARKPDLV
VLAEKFMVIE DAENLWFSEY FSKNKITFSG SDRETLKFDS DKASAKIHLA NMRIKTARHF
TALPKQFLSQ KSLPLAFPLF IKSIDATNGN GIDELSYVNN FAEFEAKVLS IYTEFEQPAL
VEEYLPGRDF TVAIICNSSG GMTVSSIEIL RPEDQQQNTE CCMQVGVYDD SHKVNELAKA
AFLGLGLRDF ALIDVRMNKY GQCFFMGANL VPNMATGTSY FLRACEIANQ LSYDQVICLL
LEEFSSRSRG EKIHYQVLKQ RNLHWPRASV KIGF
//
