ID A0A1W9R261_9BACT Unreviewed; 736 AA.
AC A0A1W9R261;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=B6D64_06240 {ECO:0000313|EMBL:OQX78592.1};
OS Bacteroidetes bacterium 4484_276.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1970779 {ECO:0000313|EMBL:OQX78592.1, ECO:0000313|Proteomes:UP000192605};
RN [1] {ECO:0000313|Proteomes:UP000192605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OQX78592.1}.
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DR EMBL; NATG01000095; OQX78592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9R261; -.
DR Proteomes; UP000192605; Unassembled WGS sequence.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; 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 Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003806; ATP-grasp_PylC-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR044019; Cyanophycin_syn_N.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR PANTHER; PTHR23135:SF18; CYANOPHYCIN SYNTHETASE; 1.
DR PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR Pfam; PF02655; ATP-grasp_3; 1.
DR Pfam; PF18921; Cyanophycin_syn; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 236..489
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 736 AA; 80966 MW; 6BCA64327468F587 CRC64;
MTQNTVDYKN YTVAEGPVKS EKIKVYHGAN YFSGGPVVLF RINLGEYDEV FTNEIEGFFE
KLSGLMPSLY EHFCSVGRQG GFFIRVKEGT LLGHVMEHVS IELQTLAGMD AGYGKTRSTL
TQGVYNVIFR YLDEDAGIFA GKAALNLVNS ILTGEEFDVF KIIETLIYIR EKNLLGPSTQ
AIVDECEKRQ IPWVRLDDYN LVQLGTGKYL KHIQATLTSE TSHIAVGLAA DKYLTTKMLN
EAGVPVPETV ETDNLEILLN FRNRINAPIV VKPVTGNLGE YSMINIKSDE EIASAFALAG
ESGEFILSQQ FIPGNSYRLL VINDKFVAAS QLDPPFIIGD GESTIGQLID ELNTQPGRDW
GDKGKLTKVE VDKITGRIFK TNNLGLESIL PEGRKLVLKK SGNPKVGGFS TDVTGKVHLM
NKYFAERAAK SIGLNIAGVD IICADISKPI HKTGGTVIEI NAAPDFRMHL KPAAGKSRKV
ALPMLDMLFP ADAPNHIPIL SVTGSTGKTL TTELLNFCFQ AAGFSTGLAN SKGLFLDGKE
IFTGDATFPE FAKTILKDRG LDCAIAETSK EGILREGIGY KFADYGIVLN VSEIDINSDD
IRYIEDLAYA QSVVAEQVYD QGFTILNADD ELVLEMRERI YSQLALISNI AINQQVLAHT
RRGGLAIYIE QENFIIHHFN KKMVLMPLSE IPPSLLGQSN PGYYELLATI AVLHAHNFEM
LQISTWIKSF KVGKGG
//