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Database: UniProt
Entry: D2Z536_9BACT
LinkDB: D2Z536_9BACT
Original site: D2Z536_9BACT 
ID   D2Z536_9BACT            Unreviewed;       497 AA.
AC   D2Z536;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=AMP-dependent synthetase and ligase {ECO:0000313|EMBL:EFC90595.1};
GN   ORFNames=Dpep_0567 {ECO:0000313|EMBL:EFC90595.1};
OS   Dethiosulfovibrio peptidovorans DSM 11002.
OC   Bacteria; Synergistota; Synergistia; Synergistales;
OC   Dethiosulfovibrionaceae; Dethiosulfovibrio.
OX   NCBI_TaxID=469381 {ECO:0000313|EMBL:EFC90595.1, ECO:0000313|Proteomes:UP000006427};
RN   [1] {ECO:0000313|EMBL:EFC90595.1, ECO:0000313|Proteomes:UP000006427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11002 {ECO:0000313|EMBL:EFC90595.1,
RC   ECO:0000313|Proteomes:UP000006427};
RX   PubMed=21304695;
RA   Labutti K., Mayilraj S., Clum A., Lucas S., Glavina Del Rio T., Nolan M.,
RA   Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Goodwin L., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S., Goker M.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Permanent draft genome sequence of Dethiosulfovibrio peptidovorans type
RT   strain (SEBR 4207).";
RL   Stand. Genomic Sci. 3:85-92(2010).
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:EFC90595.1}.
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DR   EMBL; ABTR02000001; EFC90595.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2Z536; -.
DR   STRING; 469381.Dpep_0567; -.
DR   PaxDb; 469381-Dpep_0567; -.
DR   eggNOG; COG0318; Bacteria.
DR   Proteomes; UP000006427; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   PANTHER; PTHR43767:SF10; SURFACTIN SYNTHASE SUBUNIT 1; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:EFC90595.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006427}.
FT   DOMAIN          19..357
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          407..482
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   497 AA;  54078 MW;  B8E6CD3379D21D0E CRC64;
     MEEPFRIEDR VSEVWRDGDP ILWWNGEWMT AGMLFDMAED SKMVLYGGGF RRGDRLMVLM
     PNCPALLALS IACWRLGGTV VPGNPQAGPE AVLSSIDAVD PCAVVVGAPL EGSFTSLSES
     PVPVISMSLD APLNGFRGVD TSISEDHIAL LFSTSGTTGR PKVVPVSHEN VLSDMDQALK
     QVSEISDDEV FLNVLPNFHT LGFIVSGILP LLFHFRQAIL PSFMPVDRTL RAIEASGVTA
     IVAVPTMLRF MVAASLRMGM RFSSVRLVIS GGDRFSVDLD SRIEKVFGVP VLEGYGLTEC
     SPILAVNPSY QTRKLGTVGP ILDGLEWQIR GLDGEVKEDG EEGVLWVKGP SVVSRYFRNP
     EVSAEKFVDG WFNTGDVVSI DGDGYVSIMD RAGDMIIVGG FNVHPQEVEA VLSSYPGVKE
     AVVVGKENSF SGQIPCGYVI LDPSASVTSA ELISYCKGHL PHYKVPRKIE TVEDFPRNSL
     GKVLRRVLRD NLNRGSR
//
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