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Database: UniProt
Entry: B8G0B5_DESHD
LinkDB: B8G0B5_DESHD
Original site: B8G0B5_DESHD 
ID   B8G0B5_DESHD            Unreviewed;       396 AA.
AC   B8G0B5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   OrderedLocusNames=Dhaf_4856 {ECO:0000313|EMBL:ACL22851.1};
OS   Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564 {ECO:0000313|EMBL:ACL22851.1, ECO:0000313|Proteomes:UP000007726};
RN   [1] {ECO:0000313|EMBL:ACL22851.1, ECO:0000313|Proteomes:UP000007726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10664 / DCB-2 {ECO:0000313|Proteomes:UP000007726};
RX   PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA   Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA   Tiedje J.M.;
RT   "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT   anaerobe capable of dehalogenation and metal reduction.";
RL   BMC Microbiol. 12:21-21(2012).
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DR   EMBL; CP001336; ACL22851.1; -; Genomic_DNA.
DR   RefSeq; WP_011462268.1; NC_011830.1.
DR   AlphaFoldDB; B8G0B5; -.
DR   KEGG; dhd:Dhaf_4856; -.
DR   HOGENOM; CLU_707177_0_0_9; -.
DR   Proteomes; UP000007726; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0071524; P:pyrrolysine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003806; ATP-grasp_PylC-type.
DR   InterPro; IPR023890; Pyrrolys_PylC.
DR   NCBIfam; TIGR03909; pyrrolys_PylC; 1.
DR   PANTHER; PTHR43055; FORMATE-DEPENDENT PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR   PANTHER; PTHR43055:SF1; FORMATE-DEPENDENT PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR   Pfam; PF02655; ATP-grasp_3; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          84..279
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   396 AA;  44518 MW;  61ABAB0DDA62A28F CRC64;
     MRVGIIGGKL QGVEAAYLAK KAGWDVVLFD RRKKAQGAQL ADVFHCMDIL RSREEFVAEL
     KGVNLILPAI EDLEVLTALA DIGQRTHIPC VLDLDAYRIS SSKQRSNQLF AAMGVPAPRP
     WPDCHFPMLL KPSDGSGSEG VQVIPCREKL ERLLHQESRD NWVLEEYLEG PSYSIEVMGF
     SGNYQVFQIT ELEMDAQYDC KRVLAPARLD LGLKREFEEM ALKLAGELSL QGIMDVEVIL
     HAGKLKVLEI DARLPSQTPI AVFHSTGFNM VEYLGKAFVQ GKMPGPRLKR ARQKGAEKPV
     ILEHFLVTPE KIEACGEHIL GEAGPLHVLR DFFGADEVLT DYTWGKKEWV LTLMTWGSSP
     VEVWAKRDQV LKRIQEELQI PEVLDPYPPS WYEGAE
//
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