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Database: UniProt
Entry: D5V0Q3_ARCNC
LinkDB: D5V0Q3_ARCNC
Original site: D5V0Q3_ARCNC 
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
//
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