ID Q2Y7Z3_NITMU Unreviewed; 1574 AA.
AC Q2Y7Z3;
DT 20-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2005, sequence version 1.
DT 24-JAN-2024, entry version 114.
DE SubName: Full=Acyl transferase domain-containing protein {ECO:0000313|EMBL:SEG15779.1};
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:ABB75128.1};
GN OrderedLocusNames=Nmul_A1831 {ECO:0000313|EMBL:ABB75128.1};
GN ORFNames=SAMN05216403_1385 {ECO:0000313|EMBL:SEG15779.1};
OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=323848 {ECO:0000313|EMBL:ABB75128.1, ECO:0000313|Proteomes:UP000002718};
RN [1] {ECO:0000313|Proteomes:UP000002718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25196 / NCIMB 11849 / C 71
RC {ECO:0000313|Proteomes:UP000002718};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT 25196.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABB75128.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB75128.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Richardson P.;
RT "Complete sequence of Chromosome 1 of Nitrosospira multiformis ATCC
RT 25196.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ABB75128.1, ECO:0000313|Proteomes:UP000002718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB75128.1}, and ATCC 25196 /
RC NCIMB 11849 / C 71 {ECO:0000313|Proteomes:UP000002718};
RX PubMed=18390676; DOI=10.1128/AEM.02722-07;
RA Norton J.M., Klotz M.G., Stein L.Y., Arp D.J., Bottomley P.J., Chain P.S.,
RA Hauser L.J., Land M.L., Larimer F.W., Shin M.W., Starkenburg S.R.;
RT "Complete genome sequence of Nitrosospira multiformis, an ammonia-oxidizing
RT bacterium from the soil environment.";
RL Appl. Environ. Microbiol. 74:3559-3572(2008).
RN [4] {ECO:0000313|EMBL:SEG15779.1, ECO:0000313|Proteomes:UP000236751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nl13 {ECO:0000313|EMBL:SEG15779.1,
RC ECO:0000313|Proteomes:UP000236751};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000103; ABB75128.1; -; Genomic_DNA.
DR EMBL; FNVK01000038; SEG15779.1; -; Genomic_DNA.
DR RefSeq; WP_011381148.1; NZ_FNVK01000038.1.
DR STRING; 323848.Nmul_A1831; -.
DR KEGG; nmu:Nmul_A1831; -.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_35_4_4; -.
DR OMA; DININHS; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000002718; Chromosome.
DR Proteomes; UP000236751; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; INACTIVE PHENOLPHTHIOCEROL SYNTHESIS POLYKETIDE SYNTHASE TYPE I PKS1-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF21394; Beta-ketacyl_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002718};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SEG15779.1}.
FT DOMAIN 12..442
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1492..1567
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1574 AA; 171589 MW; DB37525C6301CA00 CRC64;
MDHTEEFSER DDIDIAIIGM AGRFPGADNV DTFWRNLQDG VESVTFFTDE ELLARGISRK
TLEDPHYIKA GAELPGVDLF DASFFGYTPR EAAETDPQHR LFLEVAWQAL EDAGYDASNC
RVPVGVYAGC GVNTYLLLNL FSSGRFSDMH DISSLQGLMN GNNKDSMTTT VSYKLNLRGP
GITVQTACST SLAAVHVACR GLLNHEADMA MAGGVWVNLL HEGGYRYQPG AILSPDGHCR
AFDTNAAGTV IGSGVGIVVL KRLADALADG DTIHAVIKGS AINNDGSAKV GYTAPSVEGQ
AEVILAAQAI AGVDADTISY VETHGTGTTI GDPIEIAALT QAFRESTDKR GFCAIGSVKT
NVGHLDAAAG VAGLIKTVLA MKHRTLPPSL NFEQPNPQID FSSSPFYVNT ESRHWSNESA
PRRAGVSSFG IGGTNVHVVL EEAPPVEPVS SSRACQLLTL SARTRTALDA MIAGLHEHLR
AHPGLPLADA AYTLQTGRKG FACRAVVLCH DRNEALGVLE RKPADRFVTG QVASENRPIV
FLFPGQGAQH IDMAWELYHG EAVFRREFDR CVELLQPHLN FDLRTALYPN LDPNLEGGDE
ARKKELSARL EQTEVTQPAL FAVEYALAQL WMSWGIQPAA MIGHSVGEYV AACLAGIFSL
KDALRLVALR GRLLQQTETG AMLAVMLPEA EITPYLSESC DLAAVNGPEL CVLSGPVAAI
EALETDLRNK GVEARRLHVS HAFHSAQVEP MLPAFMELIS AMELHPPQIP FLSNLSGDWI
TSQEATDPGY WRQHVRGTVR FDDGLRELLG NPNRILLEVG PGETLTTLAR RHSEAKPEHL
ILSSLPHPGR ANQSQAHFYL CLGRLWLAGV DIDWRSFYAD ERRRRVSLPT YPFERQSYWI
KPGNQKTAKT AKAVGEEDRP RLMAGLEPGA RRQVRDNAGP VVRPLDEWFY TPSWRRSDSI
EQESILLDQG RSFILFADDH PFGVALTGHL LTLGIKPIVV SAGPAFYRQD KDHYVVRPGE
RQDYDLLLRN IDEDGRTLGH IFHLWSLTGN GGGRIYRESQ VENQVEIEAR NFFSLFYLAQ
ALESAKQVIP SEAKVEIMVI TDQFEDVTGS ESLRPEKALL LGPCKVIPQE YAYLSCRLVD
IELPAGDGTA KNRLVHQIVA ESQAEPVSSM VAYRGPHRWI QTFEPIQCGK PGKAHLRLRN
GGVYLITGGL GGIGLTLAEH LTRNYRAKLV LMGRSLLPAR EQWSNVISAA EKADRTRSKI
EKVMHLEALG AEVLVLQADV AIQAELKTAV TQAYEHFGAI HGVIHSAGEV GTDLISVKNG
GEVAKVFAPK VQGTQALQAV FRDASLDFML LCSSLAAIAG GLSKVDYCAA NAYLDAVARG
ATRSAHSGFT FPVISVNWDG WRDVGMAANM AMPEGMGISP REGAEAFEHI VNNVVRPQVI
VSTLDLHARL NQTQEDLVTL VGEPFALAEN GQHEQGGQPH YPRPALDTAF VAPESDLEKS
IAEIWQSLLG MDAVGIHDNL FELGGDSLLG IQLLSRVRAV FGIDMRPADF FRSPTVAGLA
ELVETKLLDE IECL
//