ID C0Q8U4_DESAH Unreviewed; 339 AA.
AC C0Q8U4;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 02-APR-2025, entry version 70.
DE SubName: Full=DdlB1 {ECO:0000313|EMBL:ACN14434.1};
DE EC=6.3.2.4 {ECO:0000313|EMBL:ACN14434.1};
GN Name=ddlB1 {ECO:0000313|EMBL:ACN14434.1};
GN OrderedLocusNames=HRM2_13230 {ECO:0000313|EMBL:ACN14434.1};
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
OC Desulfobacterales; Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN14434.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN14434.1, ECO:0000313|Proteomes:UP000000442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC {ECO:0000313|Proteomes:UP000000442};
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR EMBL; CP001087; ACN14434.1; -; Genomic_DNA.
DR RefSeq; WP_015903221.1; NC_012108.1.
DR AlphaFoldDB; C0Q8U4; -.
DR STRING; 177437.HRM2_13230; -.
DR KEGG; dat:HRM2_13230; -.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_039268_2_0_7; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000000442; 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 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:SF23; D-ALANINE--D-ALANINE LIGASE B; 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:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ACN14434.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000000442}.
FT DOMAIN 111..329
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 339 AA; 36736 MW; 518EBE905CC45244 CRC64;
MNKTIAIVHN RINNGSLPDE IDVLVQVDAV SQALSGLGYE PIAVPCDLDL NALKQTLTAM
KPAVVFNLVE SLDGHGRLIQ VVPALVEALG YACTGCPAEA IYLTSHKVMA KERMRSLGLP
TADWINPVPL DIPWQGAADL GPTGTWIIKS LWEHASLGLE LENLVKGNSR EIAALLPDRA
SALGGACFAE QFIQGREFNL SLMDTDKGVR VLPPAEIIFK GFDHDQPKIV GYRAKWVQDA
AEYHNTPRSF DFSPKDAPLI ANLERLSLGC WHGFGLRGYA RVDFRVDDLG NPFILEVNTN
PCISPDAGFC AALEQAGISH GQGIHMILKQ SSQPIPAMG
//
