ID B4HFJ4_DROSE Unreviewed; 1561 AA.
AC B4HFJ4;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase {ECO:0000256|ARBA:ARBA00016301};
DE AltName: Full=4'-phosphopantetheinyl transferase {ECO:0000256|ARBA:ARBA00030484};
DE AltName: Full=Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase {ECO:0000256|ARBA:ARBA00033443};
GN Name=Dsec\GM25331 {ECO:0000313|EMBL:EDW41225.1};
GN ORFNames=Dsec_GM25331 {ECO:0000313|EMBL:EDW41225.1};
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238 {ECO:0000313|Proteomes:UP000001292};
RN [1] {ECO:0000313|EMBL:EDW41225.1, ECO:0000313|Proteomes:UP000001292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25
RC {ECO:0000313|Proteomes:UP000001292};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + apo-[ACP] = acetyl-[ACP] + adenosine 3',5'-
CC bisphosphate + H(+); Xref=Rhea:RHEA:46564, Rhea:RHEA-COMP:9621,
CC Rhea:RHEA-COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:58343, ChEBI:CHEBI:78446;
CC Evidence={ECO:0000256|ARBA:ARBA00023959};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46565;
CC Evidence={ECO:0000256|ARBA:ARBA00023959};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-
CC [ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7;
CC Evidence={ECO:0000256|ARBA:ARBA00023952};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12069;
CC Evidence={ECO:0000256|ARBA:ARBA00023952};
CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.
CC {ECO:0000256|ARBA:ARBA00006195}.
CC -!- SIMILARITY: Belongs to the neurexin family.
CC {ECO:0000256|ARBA:ARBA00010241}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; CH480815; EDW41225.1; -; Genomic_DNA.
DR RefSeq; XP_002030239.1; XM_002030203.1.
DR SMR; B4HFJ4; -.
DR STRING; 7238.B4HFJ4; -.
DR EnsemblMetazoa; FBtr0208316; FBpp0206808; FBgn0180191.
DR HOGENOM; CLU_003504_1_0_1; -.
DR OMA; CIVAIMS; -.
DR PhylomeDB; B4HFJ4; -.
DR Proteomes; UP000001292; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblMetazoa.
DR GO; GO:0005919; C:pleated septate junction; IEA:EnsemblMetazoa.
DR GO; GO:0048786; C:presynaptic active zone; IEA:EnsemblMetazoa.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008366; P:axon ensheathment; IEA:EnsemblMetazoa.
DR GO; GO:0061343; P:cell adhesion involved in heart morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0007391; P:dorsal closure; IEA:EnsemblMetazoa.
DR GO; GO:0060857; P:establishment of glial blood-brain barrier; IEA:EnsemblMetazoa.
DR GO; GO:0003015; P:heart process; IEA:EnsemblMetazoa.
DR GO; GO:0021682; P:nerve maturation; IEA:EnsemblMetazoa.
DR GO; GO:0097105; P:presynaptic membrane assembly; IEA:EnsemblMetazoa.
DR GO; GO:0035151; P:regulation of tube size, open tracheal system; IEA:EnsemblMetazoa.
DR GO; GO:0019991; P:septate junction assembly; IEA:EnsemblMetazoa.
DR GO; GO:0008039; P:synaptic target recognition; IEA:EnsemblMetazoa.
DR GO; GO:0072553; P:terminal button organization; IEA:EnsemblMetazoa.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00110; LamG; 4.
DR Gene3D; 2.60.120.1000; -; 1.
DR Gene3D; 2.60.120.200; -; 4.
DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR PANTHER; PTHR15036:SF49; AXOTACTIN; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF01648; ACPS; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF02210; Laminin_G_2; 4.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00282; LamG; 4.
DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001292};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..1561
FT /note="L-aminoadipate-semialdehyde dehydrogenase-
FT phosphopantetheinyl transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002808675"
FT TRANSMEM 1495..1515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..462
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 466..646
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 652..817
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 819..856
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1073..1239
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1240..1276
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1280..1460
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
SQ SEQUENCE 1561 AA; 176993 MW; 95C23833D18A2318 CRC64;
MRPPRSNTKA AFSSLQFGLL CLLLLVNNGI ESVQADAFTD YFSDYDCNQP LMERAVLTAT
SSLTERGPDK ARLNVKFARD VRGKPYWVTG KDYDGPPLSF NVSHQGSMVL LAGIAGESSD
PDFGIGTDVM KIEYSGGKSL SEFFRLMKSK FSTEEWSYIG RPHHDEREQV KAFMRHWCLK
EAYVKELGVG ITVELQKISF SVDTTRSLET EVSPLIGTSL RCHDQPMDNW HFEEHLLQED
YCAAIAFRNC LPQEHGRFKF LQVEELLVKT GTSWSAKNSD FDQRLIIDLG VVRNVTHIAL
QGRPHSNEYV TEYTISYGIT DLEFADYKEP GGNVKREWIA FGGGLLHRKE TSNAAWTPVE
NTYNHFLTLD LGDPRTVRKI ATMGRMHTDE FVTEYIVQYS DDGEFWRSYV NPTSEPQMFK
GNSDGNSIHY NVFEVPIIAQ WVRINPTRWH DRISMRVELY GCDYISENLY FNGTGLVRYD
LRREPITSTK ESIRFRFKTA FANGVMMYSR GTQGDYYALQ LKDNKMVLNL DLGSRVMTSL
SVGSLLDDNV WHDVVISRNQ RDIIFSVDRV IVRGRIQGEF TRLNLNRELY LGGVPNVQEG
LIVQQNFSGC LENIYFNSTN FIRVMKDSTE LGEGYLFTRV NTIYACPSPP IYPVTFTTRS
SFVRLKGYEN SQRLNVSFYF RTYEETGVML HHDFYSGGYL KVFLEFGKVK IDLKVKDKAR
IILDNYDDQF NDGKWHSFVI SIEKNRLILN IDQRPMTTTK SLQVATGAQY YIAGGKDKNG
FVGCMRLISV DGNYKLPQDW VKGEEVCCGD DVVVDACQMI DRCNPNPCQH KGLCHQNSRE
FFCDCGHTGY AGAVCHTSNN PLSCLALKNV QHVQQRVNLN LDVDGSGPLE PFPVTCEFYS
DGRVITTLSH SQEHTTTVDG FQEPGSFEQS IMYDANQLQI EALLNRSHSC WQRLSYSCRS
SRLFNSPSEA GNFRPFSWWI SRHNQPMDYW AGALPGSRKC ECGILGKCHD PTKWCNCDSN
SLEWMEDGGD IREKEYLPVR AVKFGDTGTP LDEKMGRYTL GPLRCEGDDL FSNVVTFRIA
DASINLPPFD MGHSGDIYLE FRTTQENSVI FHATGPTDYI KLSLNGGNKL QFQYQAGSGP
LGVNVGTSYH LNDNNWHTVS VERNRKEARL VVDGSIKAEV REPPGPVRAL HLTSDLVIGA
TTEYRDGYVG CIRALLLNGK MVDLKDYSKR GLYGISTGCV GRCESNPCLN NGTCIERYDG
YSCDCRWSAF KGPICADEIG VNLRSSSIIR YEFEGSFRST IAENIRVGFT TTIPKGFLLG
FSSNLTGEYL TIQISNSGHL RCVFDFGFER QEIIFPKKHF GLGQYHDMHF MRKNGGSTVV
LKVDNYEPVE YNFDIKASAD AQFNNIQYMY IGKNESMTDG FVGCVSRVQF DDIYPLKLMF
QQNPPKNVKS LGTQLTEDFC GVEPVTHPPI EIETRPPPLV DEEKLRKAYN EVDSVLLACL
LVILFLLLIL MFFLIGRYLH RHKGDYLTHE DQGADGADDP DDAVLHSTTG HQVRKRTEIF
I
//
