ACSF4_DANRE
ID ACSF4_DANRE Reviewed; 1149 AA.
AC Q5RG49;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Beta-alanine-activating enzyme {ECO:0000250|UniProtKB:Q80WC9};
DE EC=6.2.1.-;
DE AltName: Full=Acyl-CoA synthetase family member 4;
GN Name=aasdh; Synonyms=acsf4; ORFNames=si:dkeyp-117h8.3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Covalently binds beta-alanine in an ATP-dependent manner to
CC form a thioester bond with its phosphopantetheine group and transfers
CC it to an, as yet, unknown acceptor. May be required for a post-
CC translational protein modification or for post-transcriptional
CC modification of an RNA. {ECO:0000250|UniProtKB:Q80WC9}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CR352243; CAI21316.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5RG49; -.
DR SMR; Q5RG49; -.
DR STRING; 7955.ENSDARP00000118390; -.
DR PaxDb; Q5RG49; -.
DR ZFIN; ZDB-GENE-041210-322; aasdh.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG4649; Eukaryota.
DR InParanoid; Q5RG49; -.
DR PhylomeDB; Q5RG49; -.
DR TreeFam; TF314245; -.
DR PRO; PR:Q5RG49; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016878; F:acid-thiol ligase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 3.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 7.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Nucleotide-binding; Phosphopantetheine; Phosphoprotein; Reference proteome.
FT CHAIN 1..1149
FT /note="Beta-alanine-activating enzyme"
FT /id="PRO_0000315805"
FT DOMAIN 570..646
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 653..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 605
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1149 AA; 125506 MW; A8790D43ED0B8FC2 CRC64;
MTAKLLYELV HEAARAHGDK RAVAFDSSIA ARVSLTYDEL IFMSDELTAQ LRVSVQNHEG
AIGLFCHPDV LLPVWIIGIL QFPAAYLPLD PASPPQCSLR MINNCRLSFC LIQNELLHSA
FSILISVEVC ATFCSHRLTL IKIKSEQKEN SQANDAPFSS AVTKNIQQGE PLAYILHTSG
TTGLPKIVKV PHRCIVPNII HLRSVFKMTP EDVVFLSSPL TFDPSVVEVF LALSSGACLL
IVPSAVKKMP RRLAHVLFKR NTTTVLQATP TLVRRFGKVV LQEEVLSADS SLRILAFGGE
PCPSLNLVKS WRQEGNRTHI YNLYGTTEVS CWASWYKVPD EHLCLEDITD APVPLGEPML
DTVMEVRDET GHLVTEGEGQ LFIGGQNRVC LLDDEETVVK GTMRATGDWV QVQNSNLYFL
GRKDRLVKRF GQRVHLDALQ QMIESFSGVE ACAVNLSKDD RLLAFIVLTS GHAGAPLSSE
IHHDKHLTQP SEISVSVSPK ASPPSLRVTE GEIRHQLSKR LSSHSIPDMM VFIPALPLTS
HGKIAIDELM KTCETQRQDK NKQAPQKDTA SVRLKLQNLW KECLGLQDDV VVEENAHFMF
SGGDSLQALR LFDDITVAMG TTSVGLLEVI LDGSFSDLLS HIMTETHDDA VLPSKKRTAD
YSDSEASGKR QHKEMTTSSD TESPFVVPSL RRTMGFVVVR RAAEVFKWGF QKIPQGIFSD
APDKNYVTNN SVGNDTGLIS NPSLELSKSS AVTNMADHLQ AQEETLLASE SPSSHGGVRE
DSTGVLPLAL RVLWRSDTGR CVDASPMLLV APDRTTVFIG SHSHRLQALD LSRGEVIWER
ILGDRLESSA AISSCGGLVA IGCYDRQMYF LDVSCGDTVW TFETGDVVKS SPTVDPKTGL
VFAGSHDGHV YALNPLTKTC TWQHYCGGGA VFSSPCVHLS PRQLYCSSLG GHLHCLNPDS
GKVLWKYSSS APFFSSPHCS DSSVFIGSVN GHIIGISHSG NTLWDFSTDG PVFSSPCISS
LTLLTNQPPS TTPSSSVTTS PNHIVTCGSH DGHVYCLNAQ NGSLLWQFQT TGKVFSTPFV
FSGALWGLRT LAAVCSTDGK VWVLDGETGI QKATLSLPGE LFSSPVIWGS KLVVGCRNDY
VYCLELTTQ
