ID A0A0D5AF36_9NOCA Unreviewed; 475 AA.
AC A0A0D5AF36;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Phosphoserine phosphatase {ECO:0000313|EMBL:AJW41393.1};
GN ORFNames=NY08_3383 {ECO:0000313|EMBL:AJW41393.1};
OS Rhodococcus sp. B7740.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW41393.1, ECO:0000313|Proteomes:UP000032410};
RN [1] {ECO:0000313|EMBL:AJW41393.1, ECO:0000313|Proteomes:UP000032410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7740 {ECO:0000313|EMBL:AJW41393.1};
RX PubMed=25931596;
RA Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.;
RT "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid-Producing
RT Bacterium Isolated from the Arctic Sea.";
RL Genome Announc. 3:0-0(2015).
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DR EMBL; CP010797; AJW41393.1; -; Genomic_DNA.
DR RefSeq; WP_032396772.1; NZ_CP010797.1.
DR AlphaFoldDB; A0A0D5AF36; -.
DR STRING; 1564114.NY08_3383; -.
DR KEGG; rhb:NY08_3383; -.
DR PATRIC; fig|1564114.4.peg.3338; -.
DR HOGENOM; CLU_027938_11_1_11; -.
DR Proteomes; UP000032410; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.20.1440.100; SG protein - dephosphorylation function; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006385; HAD_hydro_SerB1.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR01490; HAD-SF-IB-hyp1; 1.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF11; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE ALPHA; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF12710; HAD; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 4: Predicted;
FT DOMAIN 309..423
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 475 AA; 51771 MW; 55761E6AEA9AF752 CRC64;
MTEFDDRLIA IAAAPPGRDT VAFFDLDGTL INGFSARAVF LERLKTLDVT VKELWEISSA
VVEMRMRNSP VDNLMGKAVR GLEGRREEDL MEQAYTLFRN EIAPMIYPQA RALVEAHRHA
GHRLVMATSA TPYQALPVQQ DMMFETLLCT TPVVTDGILT GELVGDSLWG PRKAQAAIDY
AEREGIALAG CFAYSNGGED VPLLEAVGRP VALNPDPELQ RYAAKKKWPS LTLESPKRGT
DLTSAVRSTA ALGSVLASAS IGLGLGLLTR SRRNGANITS TIAPDIALTI AGVKLDVTGT
ENAWSARPAV FMFNHQSTAD SIIVTSILRR DITAVAKREL ERDPRFALLG RIFDVAYVDR
GDPAQAREAM RPAIEKLHSG ISVAIAPEGT RMPTSRLGRF KKGGFHLAMQ AGVPIVPIVI
HNAGDVMWKK DFTVHSGTVK VTVGEPIPTT DWEPEKIDSY VDDVRSYFDR TLGYA
//