NIFP_AZOCH
ID NIFP_AZOCH Reviewed; 269 AA.
AC P23145;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Probable serine acetyltransferase;
DE Short=SAT;
DE EC=2.3.1.30;
GN Name=nifP;
OS Azotobacter chroococcum mcd 1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1885524; DOI=10.1128/jb.173.17.5457-5469.1991;
RA Evans D.J., Jones R., Woodley P.R., Wilborn J.R., Robson R.L.;
RT "Nucleotide sequence and genetic analysis of the Azotobacter chroococcum
RT nifUSVWZM gene cluster, including a new gene (nifP) which encodes a serine
RT acetyltransferase.";
RL J. Bacteriol. 173:5457-5469(1991).
CC -!- FUNCTION: Probable serine acetyltransferase required for optimizing the
CC expression of nitrogenase activity. May be required to boost rates of
CC synthesis or intracellular concentrations of cysteine or methionine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-serine = CoA + O-acetyl-L-serine;
CC Xref=Rhea:RHEA:24560, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:58340; EC=2.3.1.30;
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
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DR EMBL; M60090; AAA22162.1; -; Genomic_DNA.
DR PIR; D43706; D43706.
DR AlphaFoldDB; P23145; -.
DR SMR; P23145; -.
DR PRIDE; P23145; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0009001; F:serine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR CDD; cd03354; LbH_SAT; 1.
DR Gene3D; 1.10.3130.10; -; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR045304; LbH_SAT.
DR InterPro; IPR042122; Ser_AcTrfase_N_sf.
DR InterPro; IPR005881; Ser_O-AcTrfase.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00132; Hexapep; 2.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR01172; cysE; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Cysteine biosynthesis;
KW Nitrogen fixation; Repeat; Transferase.
FT CHAIN 1..269
FT /note="Probable serine acetyltransferase"
FT /id="PRO_0000068689"
FT REGION 242..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 269 AA; 28578 MW; E0BBCC982E66FDBB CRC64;
MSLLAQWRED IRCVFERDPA ARTTFEVLTT YPGVHAIMLY RLAHRLWRPN ALPRPAAVVR
ARLVSNVDIH PGAVIGARFF IDHGACVVIG ETAEIGRDVT LYHGVTLGGT TGAKGKRHPT
LGDVVLVGAG AKILGPITIG ANARVGANSV VVQDVPEGCT VVGIPGKVVK LREAGQLNPY
GIDLDHHLIP DPVGKAIACL LERIDSLEKR VEAGGLVAAA ASSTFYEGCN PDNSICETNL
RRSAPWSSGR PRRPAHAGDR VSGRAKGSD