ID W8KTL6_9GAMM Unreviewed; 881 AA.
AC W8KTL6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=AMP-dependent synthetase {ECO:0000313|EMBL:AHK80372.1};
GN ORFNames=M911_15800 {ECO:0000313|EMBL:AHK80372.1};
OS Ectothiorhodospira haloalkaliphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=421628 {ECO:0000313|EMBL:AHK80372.1, ECO:0000313|Proteomes:UP000019442};
RN [1] {ECO:0000313|EMBL:AHK80372.1, ECO:0000313|Proteomes:UP000019442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A {ECO:0000313|EMBL:AHK80372.1,
RC ECO:0000313|Proteomes:UP000019442};
RX PubMed=25057327; DOI=10.7150/jgen.9123;
RA Singh K.S., Kirksey J., Hoff W.D., Deole R.;
RT "Draft Genome Sequence of the Extremely Halophilic Phototrophic Purple
RT Sulfur Bacterium Halorhodospira halochloris.";
RL J Genomics 2:118-120(2014).
RN [2] {ECO:0000313|Proteomes:UP000019442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A {ECO:0000313|Proteomes:UP000019442};
RA Singh K.S.;
RT "Draft Genome Sequence of extremely halophilic bacteria Halorhodospira
RT halochloris.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP007268; AHK80372.1; -; Genomic_DNA.
DR RefSeq; WP_025282916.1; NZ_CP007268.1.
DR AlphaFoldDB; W8KTL6; -.
DR KEGG; hhc:M911_15800; -.
DR PATRIC; fig|1354791.3.peg.500; -.
DR HOGENOM; CLU_000022_45_1_6; -.
DR OrthoDB; 5296889at2; -.
DR Proteomes; UP000019442; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 InterPro; IPR036736; ACP-like_sf.
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; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR009081; PP-bd_ACP.
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; 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 PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000019442}.
FT DOMAIN 564..640
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 881 AA; 96661 MW; 0AF22E1CFBDC11D9 CRC64;
MTASDINALL GSRELPGARE ALLEMTRDGS RSWRREELLD MAGRLSAGLT AAGLKTGDRV
ALMAPNSAPW VAVALGVMRA GGVLVPLDTQ MPGEDLAHAL NDCRPGTILT TDKLLSRLPK
QIEADVWLLD KDTTDDRSWR NLVADSPAPT RASSQDTAAI FYTSGTTGPP KGVPLSHANL
ATNVQALCDQ SLAEDRDRVL VPLPFHHVYP FTVGILTPLT LGAPLIIPYS LVGPQIVRAL
RDGEATVMLG VPRLYEAIWT ALEQRVTGRG RTAARLFHGM LRVSMMARRG PGWRLGRRLF
AGLHRRMAPR LRLVVAGGAA LDPGLGRRLQ ALGWEVATGY GLSETAPILT YNPPDRVRLE
SAGLPLPGVE LAIDGQEDAG EVMARGPNVF AGYLNLPEKS REVLDDDGWF RTGDTGWIDE
DGFLHLGGRT SAMILLSGGE NVDPEKVEKQ MEKAPEIREA GVLAHDDRLA AVVVPEPELL
REVEGDELNK RLKSAMETAT QDLPTHHRPG TLKISLDPLP RTRLGKLRRH KLEERFEDLG
EGAAPKGEAK PIDPEAMGPE DQQLLSDPSV EKAWQYLAER FHDRRLTPDS GLYQDLGLDS
LAWVDLTLAL RDRIGVEMED EAISRVQSVR DLLREVAAAG EAEQGDEQDL QTALKDPEQH
LDDAARRWLA PRGSIRQFIG LILLGITRLG IRLLYRLEVE GRIPRQGGPY VLAPRHLSAL
DPLVLTRVLT WRQIRTLYWA GWTGMMFSSR LARTFSRIVG ILPIDPGRSP RRSLALAVTS
LERGHSLVWF PEGRRSRDGR LQPFRPGIGS LLLARPAPVI PVHIEGTGKA LPPGRRWPRP
GRLRIVIGEP LEPGSLGSEP REIARHLQDA VAALGEPGDT R
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