ID B8JGJ9_ANAD2 Unreviewed; 1538 AA.
AC B8JGJ9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=AMP-dependent synthetase and ligase {ECO:0000313|EMBL:ACL64670.1};
DE Flags: Precursor;
GN OrderedLocusNames=A2cp1_1326 {ECO:0000313|EMBL:ACL64670.1};
OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=455488 {ECO:0000313|EMBL:ACL64670.1, ECO:0000313|Proteomes:UP000007089};
RN [1] {ECO:0000313|EMBL:ACL64670.1, ECO:0000313|Proteomes:UP000007089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-1 / ATCC BAA-258 {ECO:0000313|Proteomes:UP000007089};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Beliaev A.S., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-1 / ATCC BAA-258 {ECO:0000313|Proteomes:UP000007089};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Beliaev A.S., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001359; ACL64670.1; -; Genomic_DNA.
DR RefSeq; WP_012632644.1; NC_011891.1.
DR KEGG; acp:A2cp1_1326; -.
DR HOGENOM; CLU_247289_0_0_7; -.
DR Proteomes; UP000007089; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd05236; FAR-N_SDR_e; 1.
DR CDD; cd09071; FAR_C; 1.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR033640; FAR_C.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000313|EMBL:ACL64670.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 1160..1238
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1494..1538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1538 AA; 165457 MW; 1830618E4FC98F57 CRC64;
MSGHGKRTRG PHGHPHPAHP GGAPAGPPPL DVARLLAGRR VLVTGATGFV GKVALSMLLD
RYPEVGRVFV LVRPGAGGTA EGRFFDKVAP SRPFDPLRAR HGAGFEAFLR DRCVPLAGDV
SDPLLGLSEA DLARLDGLDL VINSAGLVDF DASLELALGV NVDGARHAAE LCRRTGAGLV
HVSTCFVAGN RDGVVFEDEE IAGYFPRREG VEGRPRAAAL DGADFSLDTE LADAARRIAE
VRALADDRVR QSEFRERALG RLREEGRAAA DEKALRLAIG REKRLWVSQQ LVEIGRTRAL
HWGWPNTYTY TKALGEQAIE AAGVPYAIVR PSIVESALRY PFPGWNEGFT TSAPLAFMGL
KGHRSFPAAE KAILDVVPVD LVCAGIVAAA AELQERRGTA GAARGRVFHL ASGDVNPLWA
RRAVELTALY RRRFYREREE GNRTWNRLLS RIEPYPVTRA QYEAFSAPAL AALARGAGKL
LRERAPAWGA PRLSALAHRA GEALDELTSQ LEKTEAIWAM YLPFTWDNRY VFRCAGMREL
RERLSPDDRA RIPWDPEALD WRAYWLDVHL KGMEEWVFPG LEEEAEKRVH APKAHRDLLE
LLDSACERWR DRTALRLEGA AKDRLTYGEL HALSGRVAAF LAAAGVVKGD RVLLASENRP
EWAVAYFGVL RAGAAVVPVD PKLSEPELAN LWRSAGARLA LLSDDAADAL PGLAALAAAA
VPEARVVSLG EALRGGPAVP SIRLSPDDLA SLIFTSGTTG TPKGVMLSHR NFASLVAKLV
TVFDLGPGDG MLSVLPLHHT FEFTCGLLVP LSRGAEVEYL DELTADRIGD ALGSGRVTAM
IGVPALWALL HRRITQELAA KPGVVEQAFR GLMKGNAALR DSALAWNLGK ALFWPVHRRF
GGRLRLLVSG GSALDPQVQD AFRALGFDMY EGYGLTEAAP VLAVSKPGGD APEGSVGPAL
PGIELRIADP DASGVGEVLA RGPNVMLGYW RGAAPGGQPA GVDPALSGQV LEGGWLRTGD
LGKLDPDGNL TLVGRKKDVI IDANGKNVYP DEVEERYRDD ALVKELCVVG LPDGAAEKVA
MIVVPEYGDR DRAEVRAELE AHVRAVSASL PFPQRVKVWH VFEGDLPKTS TRKVKRPLVR
EELLRLEAAA ARGRRAREES RDAQGEGWVL DLLAEVCRRP RAEIGPGSRL QAELGVDSLM
LTELSAALEE AGVPPAALEG LHAVQTAGEL ARAVGGATRR GQERAPAREA PGEKAPRAAR
DDGEIPVPAT VARLGRRVLS AGQRALYRDL YQARVVGAAH VPHDRNVLVV ANHASHLDMG
LVKVALGDEG RRLAALAAKD YFFDTPVKRA YFENFTNLIP MERDGALKAS LRAAAEALRR
GYHLLIFPEG TRTRDGAMRA FYPTAGYLAL QCDVDVLPVY LAGTHEALPP GRALPRRADL
EVRFGEPIRV DDLRARTAGL SRSDAYRAAT QVMEAAVKGL RQAWLEEHGV APAAPAAEKV
APGSAAPAAR AGTPAPAEPA APAAGPAPRH HPGRPEDA
//
