ID A7HFK5_ANADF Unreviewed; 451 AA.
AC A7HFK5;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Phospholipase D/Transphosphatidylase {ECO:0000313|EMBL:ABS27501.1};
GN OrderedLocusNames=Anae109_3316 {ECO:0000313|EMBL:ABS27501.1};
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS27501.1, ECO:0000313|Proteomes:UP000006382};
RN [1] {ECO:0000313|EMBL:ABS27501.1, ECO:0000313|Proteomes:UP000006382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS27501.1,
RC ECO:0000313|Proteomes:UP000006382};
RX PubMed=25614562; DOI=10.1128/genomeA.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
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DR EMBL; CP000769; ABS27501.1; -; Genomic_DNA.
DR AlphaFoldDB; A7HFK5; -.
DR STRING; 404589.Anae109_3316; -.
DR KEGG; afw:Anae109_3316; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_0_1_7; -.
DR Proteomes; UP000006382; Chromosome.
DR GO; GO:0030572; F:phosphatidyltransferase activity; IEA:UniProt.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:UniProt.
DR CDD; cd09110; PLDc_CLS_1; 1.
DR CDD; cd09159; PLDc_ybhO_like_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR PANTHER; PTHR21248:SF22; PHOSPHOLIPASE D; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006382};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 188..215
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 364..391
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 49445 MW; 977B3103AC9BF53E CRC64;
MRSSSAPSSG RSKPQPSSGA RPSRDAQLCS AMRAALAAGV ATGATLGVLA RRWWDLRTRY
GPWASLSAGL GEGVDSVALA LLETTATPML AGNHVERRDN GQVFDAIEET IRAARHSVHV
DVYIWKPGQP GERMVNLLCR RAREGIAVRI LVDPVGSPGF DRQLRPRLLA AGCEAHYFRP
LHERPLAFTG RNHRKLVVVD GRVGFTGGFG IAPEWLGNGL SPREWRDSNA RVEGPVVRQM
QVAFASHWLE TGGTILPAGE FERARPAGDA RAAYVTSMDV KGLSHARWVT HVAVAAARRR
AWIANAYFVP PPEVLAALCA RPERGIEVRL LLPGPYQDHP GVTFVQRRLY PCLDRSRVKV
HEYQPSMMHA KTMLIDDRLV VIGSMNLDFL SMNWLEEGCL VVDDRPFAAE FEECWRMDMA
RSRQVTGRRE PSGAGLPLAE VRPGAAPGGA P
//
