ID D5V0Q3_ARCNC Unreviewed; 3238 AA.
AC D5V0Q3;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:ADG93865.1};
GN OrderedLocusNames=Arnit_2213 {ECO:0000313|EMBL:ADG93865.1};
OS Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG
OS 7604 / NCTC 12251 / CI) (Campylobacter nitrofigilis).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Arcobacter.
OX NCBI_TaxID=572480 {ECO:0000313|EMBL:ADG93865.1, ECO:0000313|Proteomes:UP000000939};
RN [1] {ECO:0000313|EMBL:ADG93865.1, ECO:0000313|Proteomes:UP000000939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33309 / DSM 7299 / CCUG 15893 / LMG 7604 / NCTC 12251 / CI
RC {ECO:0000313|Proteomes:UP000000939};
RX PubMed=21304714; DOI=10.4056/sigs.912121;
RA Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., Bruce D., Tapia R.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Arcobacter nitrofigilis type strain (CI).";
RL Stand. Genomic Sci. 2:300-308(2010).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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DR EMBL; CP001999; ADG93865.1; -; Genomic_DNA.
DR RefSeq; WP_013136010.1; NC_014166.1.
DR STRING; 572480.Arnit_2213; -.
DR KEGG; ant:Arnit_2213; -.
DR eggNOG; COG0300; Bacteria.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG2226; Bacteria.
DR eggNOG; COG3319; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_225363_0_0_7; -.
DR OrthoDB; 5349841at2; -.
DR Proteomes; UP000000939; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd19535; Cyc_NRPS; 1.
DR CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR025110; AMP-bd_C.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 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; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000939};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..427
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1789..1863
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2873..2947
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 3238 AA; 366217 MW; 24FEDDE0A0E06911 CRC64;
MNYKNISDNP DAIAVIGMSG IFPQAKDINK YWDNLINGVE SIIQFSNEES STKGHFVRAA
ATVDDIDCFD AKFFNYSAYE AEILDPQQRL FLECCWHALE EAGYSPDKAG NVGVFAGSNI
STYLLLAQQS ILAKGDTTHL LQLLMGNDKD YLATRVSYKL NLTGPSICVQ SACSTSLLSI
HTAVQSLLNG ECKMALAGGV NISIPQELEY EYKEGMIFSP DGHCRAFDAD AKGTVAGNGV
GAVVLKPLSD AIEDGDSIHA VILGSAVNND GARKIGYTAP SIEGQSSVIA QAIALADIPV
NTIDYIETHG TGTPLGDPIE IRSLSQVFQN ETKEKGFCAI GSVKPNIGHL NCAAGIASFI
KTVLSLKNAQ IPPSLHYKKA NPEIDFINTP FFVNDKASLW PKRNHPRRAG VSSFGFGGTN
VHMILEQAPE KIETNIKKDD EINLVVLSAQ SQKQLHTLAE DYNNYLQNTE ESLQNISFTS
IEGRNHHNER LAIVAKNHNH LKQQVQEFLN TKENIQGYIG TKNYSTKIAC LFTGQGSSYP
NMAKELYTSN KLFHKNLNLC AKELENLLDI PLIDLIFGKE EHTNLLTQTK YAQPAIFAIE
YSLYNMYRGM GIEFSVLAGH SVGEIVAACV ADVFNLKDAL KLITSRGQLV QNLETNKGGM
LAIFTNQEII DKYINIYPQL SIAAHNGPNH FVLSGENIIL EKLIEQLDKD NIEYSKLKVS
HAFHSSLLDP ILDDFEKLVA SFDMKIPNTQ IVSNLYGRIV KNEEITTAKY WREHMRKPVL
FMESINTLEN MDINCFLECG PHPVLTNMGK KCVSNTDYQW IHSLQRNQED KKIILSAVAQ
LYCKGIDIQW EGLAHNKDYQ RVSLPTYPFD KQKYWLSTVA DSLQTHKQDG PLTIWNNILS
SGNKQAKEGS KALNISQLKY DEKVLITLAQ SFIIKALRSL DLFTDDKKYS LDSILQKVIP
QYHQLIQRFL EELNVVGLLK SKDKQFWQLK DINNQIIKEQ KNDCKDVFLA NPAFESVFIN
SGEQLADVLS GKTKAIDAMM METSIDEAKE IYADLPTSYY FNALLRETVK SWVSNMPNNI
PLKILEIGAG TGATSEQLLP LLPKDRSTYY YTDVSPIFLQ RANKNFEEYN FVNYTLFDIN
KNPKEQGLDY NSFDLIIASN VLHAADDLQH TMNNVSKLLK PNAMLFMYEI IKETLIGELT
TGLLLPIVKD TELRGMQPFM TKNQWESLLI KLGFKNFHSI PEENTDTSFI GERILLAQQK
EVISEEKEYN NYFHHIQWDK NEVPIEKINH LLKESSNWLI CSDKVGYTQE LTSLLKQHNQ
NVSNIELDIS SKLLNEKIKE TFNNNKPVQI LYLWGVENIS LNQLSGSQLQ EKQAVSSLKL
LDILSALSQI NLKNLKNLSI ITNGSQHTSA IPNQNIALSQ ATLWGFSQVV ALGHPELKVK
LIDFDTEMSI KDNSIDLLKN LLSKNNSNEY QLILRKNNCY LPRIRSLENT DITPTIQKVN
IDANGWYVIA GGLGGLGLKT ASWLIENGAK NILLIGRSKP NIQAKEEIDN FTKLGINIKV
AQLDITDYES LEKLINNLDL PLKGVIHSAV VRDTKTLGEM SQKERTLAVI SPKLEGAWNL
HKITQNHKEL DLFILYSSSV SLIPARGLPE YVASNAFLDA LAHYRKSKNL PAISISWGAW
AEVGTVANTS QEEQLRQNGL NSIGVKQSFN CLEQIITGDF KDTHMGIFDV NWNKLLQNHP
KNQLSSYFKD VLTVSYIEQK QGSEENLAQQ QHKLLENLKS SKNSGQSLEF ISDYLKQKIS
VLLRINVDDV PSEKDLLHLG IDSLMFLDLL NNLNQVLQIK VKPNEVMANL NINAISEHLL
KAMQSTNHSD IAELLLVDKD SLTKPFPLTD IQQAYWIGRD QHMDLGNIAC HGYMEIECKD
LDIALLEDAW NKLIQRHEML CCIIHPYGQQ QILDNVKEYH FEVRDFSKTA KKVSDKALEE
IRTELSHRVP QTDKWPLFDI HATKLQNNVT RLHISLDNIM TDGRSIGIML SEWVHIYNNP
QDTLPNLSLT FRDYIMTFEA YKQTEDYHKA KKYWVDRLDE IYPSPQLPLA KDPSKVSTPK
FIRREFHLSE EKWQILKSLG AQKAGLTPSG ILLSVYAQVL SLFSNSAKFT LNVPTFNRLA
VHPQVNDIIG EFTSLILLSV DFSKQLSFKE QANILQKQLL KDQSYDSFSG VSVMRELAKH
SKQANMPVVF TSTFGLAENV NTTFSEHESQ AKELGKQIYT ISQTPQVYID NHVHDYGGSL
NVYWDCVDEL FPEGMLDSMF EAYGNLLEQL ANNEQVWEST QAIKIPISQE QKRIQYNNTQ
NFDYLPKQDD LLSGFLRQVK QSPNHSALIT NNENLSYKEL FERSCFFAWQ LQESDINPLE
KVAIILPKGW QQISSIIATL GVNGTYVPFD YKLPEKRLLQ LLEVAKISYV ITSKEMKDNF
TWPKNIKLIT TPSNWGKEEE KIVQNNNIEF MPSNNQQLAY IIYTSGSTGI PKGVMISHHS
ALNTILDIND RFKITSDDIV FGLSGVHFDL SVYDIFGTLN AGACLVLPNE EGTKDPNHWI
DLIEKHKITI WNSVPALCEM LLIQTNANKV TMQEMRLVLL SGDWIPLSLK DKLQKSTKNA
KLYSLGGATE ASIWSIYYPI EDIDPTWNSI PYGRPLANQQ FYVLNEKYND CPQLVIGDLY
IGGEGLFMGY WQDEGKTKES FIIHPISGEK LYKTGDKGRF HPNGYIEFLG RNDLQVKING
HRIELGEIES SLLQNELIQN VVVTAIDTYG NSEISTSIKD NKQKLIAYCV CKEKNLSEIE
SKLKIWTKER LPNYMVPNHF FILNSIPLTK NGKLDRKALP LPSNEKKEIK SSTPQTENEK
LLLSICREIL QVDDINIHSD FFDIGGDSLQ ATRLSISLQK EGFNLSVNQI FMNPFLEDMA
QFIKAQNDSS LENKKQEMIS LEFNNSSSIL TSFNTISEEK PNIFCIHGSD GGVFVFNELA
DQLENDFNIY GIAAQSTIEK NNISDIASSY LEQINTRDTA YPPIICGFSS GGFVAWEIAR
QLKERGEDLT QLILIDTQFL PQELKDNSLL ILVLFALSFN MNIELLPIKE ELIVKLKNNT
YTNSELNEIQ KLNEEEFEDL FEQLIDSNSL LNNDSTNLRR KFNIFKQYVE FTIEYDMPHL
SSVDTLLLQA KQSVKNHQSW NSFGDKIQHI EVDGNHMSCL QYPNVSSISN TIQNFSKK
//