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Database: UniProt
Entry: A0A3Q1H349_9TELE
LinkDB: A0A3Q1H349_9TELE
Original site: A0A3Q1H349_9TELE 
ID   A0A3Q1H349_9TELE        Unreviewed;      1096 AA.
AC   A0A3Q1H349;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Aminoadipate-semialdehyde dehydrogenase {ECO:0000313|Ensembl:ENSAPOP00000034167.1};
GN   Name=AASDH {ECO:0000313|Ensembl:ENSAPOP00000034167.1};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000034167.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000034167.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   AlphaFoldDB; A0A3Q1H349; -.
DR   STRING; 80966.ENSAPOP00000034167; -.
DR   Ensembl; ENSAPOT00000029704.1; ENSAPOP00000034167.1; ENSAPOG00000023212.1.
DR   GeneTree; ENSGT00440000033811; -.
DR   InParanoid; A0A3Q1H349; -.
DR   OrthoDB; 76882at2759; -.
DR   Proteomes; UP000257200; Unplaced.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.480; -; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR036736; ACP-like_sf.
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; 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   PANTHER; PTHR44394; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR   PANTHER; PTHR44394:SF1; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF13360; PQQ_2; 2.
DR   SMART; SM00564; PQQ; 7.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT   DOMAIN          580..656
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          479..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..517
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..687
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1096 AA;  118637 MW;  EF95A68FF5D9199B CRC64;
     MSPRTLQQLV AAAASLYPDR AAVTYSGSVS GAPETLLYRD VAQLAGELSG ILQKNCSPNN
     GLIGLYGGED VLIPVWILGI LQSSAAYVPL DPEAPGLLSA RVMSQCGLKY CAVKTDLLQQ
     FQTALVEHAT VEVCVELPKF KLTLIRNGHL PVTEHKRGSR SPTSDDAVDA GCTDLAYVLH
     TSGTTGLPKT VRVPHKCILP NILHLRSLFQ MRADDVVFLA SPLTFDPSVV DIFLALSSGA
     RLLIVPALIK KMPNRLAQLL FKDHKATVLQ VTPTVLLRFG HRILKQDVLS SDSSLRVLAL
     GGEACPSPAL LRSWRHEDNK TCIYNIYGVT EVSCWACCYQ IPESLLQSSN ITMPSVPLGS
     PLMDTVVEVR DERGCVVTEG EGQVFIGGED RVCLLDDEDA VVAGTMRATG DWATVEDAQL
     YYQGRKDRML KRNGKRLNLD GLQQLLLSLP QVDACAVGLY EGVRLLAFIV ASTSGDHTAA
     STSSSVQQRA EQTPSALTEH QEKPPSSTEH HVEENGADRD LKRVILSQLS LLLPPHSVPD
     TLVLVPALCL TPHGKVDMEA LVKIYERKRK PLKSSWEDAS KLKQTLQALW QDTLGLAADA
     TLDEESNFLF SGGDSLKALR LSEDIHSAVG VTSPELLAVI LDGTFADVLH HVAKLTQMLS
     PESISSPPSE AKKRRTDPPS VARVKKKRKD FTAAERFQVE KRAVKVIRRA GEIIELNFRN
     TENNKSIQAD KLGEINSGNK HRDVDVGLSL SWSSDTGRCV DASPVLLVED EANQRSKTTV
     FIGSHSHRIQ SLDLTTGSLL WERVLGDRIE ASVAVSHCGS LVIVGCYDAC VHFLCAKSGK
     TRWTFETGDA VKSCPAVDPQ TGLVIVGSHD GNVYALNPQA RQCVWKRHCG GGAVFSSPHL
     SSSLRRLYVA TLGGRLLCLN PGSGDVLWSY CTDVPLFSSP SSCSGHVVIG SVDGNICCIS
     NSGKLLWRFL TKAPVFSSPC VTPDQQKLLC GSHDGRLYCL NCADGSLVWT FQTTGKVYSS
     PCVFGGSAVG RTGALVGLAS TDGSVWILDG QNGQMLASFV LPGELFSSPV VWEQSLVIGC
     RNDYVYCLKL TIEEKT
//
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