ID Q1QNT9_NITHX Unreviewed; 340 AA.
AC Q1QNT9;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 102.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:ABE62108.1};
DE EC=6.3.2.4 {ECO:0000313|EMBL:ABE62108.1};
GN OrderedLocusNames=Nham_1283 {ECO:0000313|EMBL:ABE62108.1};
OS Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Nitrobacter.
OX NCBI_TaxID=323097 {ECO:0000313|EMBL:ABE62108.1, ECO:0000313|Proteomes:UP000001953};
RN [1] {ECO:0000313|EMBL:ABE62108.1, ECO:0000313|Proteomes:UP000001953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10229 / NCIMB 13809 / X14
RC {ECO:0000313|Proteomes:UP000001953};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA Gentry M.E., Bruce D., Richardson P.;
RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000319; ABE62108.1; -; Genomic_DNA.
DR RefSeq; WP_011509800.1; NC_007964.1.
DR AlphaFoldDB; Q1QNT9; -.
DR STRING; 323097.Nham_1283; -.
DR KEGG; nha:Nham_1283; -.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_039268_2_0_5; -.
DR OMA; MQGLLEC; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000001953; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; 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; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR InterPro; IPR011127; Dala_Dala_lig_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR PANTHER; PTHR23132:SF23; D-ALANINE--D-ALANINE LIGASE B; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 1.
DR Pfam; PF01820; Dala_Dala_lig_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABE62108.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000001953}.
FT DOMAIN 127..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 340 AA; 36817 MW; DF40615B21AAC3DB CRC64;
MRITILFGGS NKERLVSVAS AQALHRALPE ADLWFWDIRD DVHNVRSEVL LDHARPFEDE
FVPGGTSMPF EQALDRARAE GRVLVLGLHG GRAENGELQA MCELRGIPFT GSGSAASHLA
FDKVAAKRFA ALAGVTTPAG VPLEEIDRAF AEHGRLIAKP ARDGSSYGLI FVNAKQDFVA
VRHAAKTEEY VIEPFVSGIE ATCGVLERSD GTVVALPPVE IVPAEGRFDY ASKYLAQTTQ
EICPGRFSSS ITARIMDHAL RAHRALSCRG YSRTDFIVTG KEPVYLETNT LPGLTAASLY
PKALKAQGIG FADFLRDQIV LAEKAGRPAH SVFSEACPRA
//