ID H6C5U8_EXODN Unreviewed; 1102 AA.
AC H6C5U8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Aminoadipate-semialdehyde dehydrogenase large subunit {ECO:0000313|EMBL:EHY59094.1};
GN ORFNames=HMPREF1120_07093 {ECO:0000313|EMBL:EHY59094.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY59094.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY59094.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY59094.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JH226135; EHY59094.1; -; Genomic_DNA.
DR RefSeq; XP_009159555.1; XM_009161307.1.
DR AlphaFoldDB; H6C5U8; -.
DR STRING; 858893.H6C5U8; -.
DR GeneID; 20311732; -.
DR VEuPathDB; FungiDB:HMPREF1120_07093; -.
DR eggNOG; KOG1178; Eukaryota.
DR eggNOG; KOG1179; Eukaryota.
DR HOGENOM; CLU_002220_2_1_1; -.
DR InParanoid; H6C5U8; -.
DR OMA; WDWLAHI; -.
DR OrthoDB; 2230730at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; ACP-like; 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 InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR PANTHER; PTHR43439:SF2; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43439; PHENYLACETATE-COENZYME A LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304}.
FT DOMAIN 612..690
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 225..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 122647 MW; B397500E2EB5E6A9 CRC64;
MQWTSSRYWA CLDKLMFLQL LKNHILFWCQ YRKSHINIIV DPRSYKMPSR ETLPAEPKVN
GVHSPNKAAL QAIFAAKART VTELISIRAK ALPDEPILGY PSHDLEYTEY TFSDLDAFPS
RLARVYSQYL PVRTSSKQDA RVVALLGPSN LDYVITALAL SRLGFTVLYL STRISEPAYL
SLLDATGCRH IVVHPTFQKT VSALKAVKPD LEIIPIRGES DYKYEPSSKL TNGVQEEQAE
QEQDLDLDEE TKKVCWIIHS SGSTGPPKPI YQTHYSALRN YEQNMNMKGF ITLPLFHAHG
LSSVFRAITS IKKIYMYNAS LPLTRQNLLK ILHQHQFEIF YGVPYALKLL SETQEGIDAL
AAMKVVMFGG SACPDALGDL LTEGGVNLVS HYGTTETGQL MTSFRPPGDK AWNYVRVHEQ
LRPYVRFEER GGNLYELVVL QGWPSKVATN REDGSYATKD LFEPHPSIPG AWKYCGRLDD
TIVLMNGEKA IPIAMEQALR HNKLVQEAVM FGAGRDQLGM IIIPSESAAD TSPEDLLDAL
WPTIEAENKA MPAYGQLARE MIKILPAGTP YPSTDKGTMI RQAFYRAFQS EIDEVYAQAE
SRAAGTLVLS EPELRDYLRK KILELDNSLQ ESDLADDTDL FSLGIDSLQS TRLRASILKD
IQLNGNTLPP NVVFEYPTIA KLAAAILSIR DSKTVEARDV IKEMEDLITK YSDFPQHVSC
PKTSTESCVV VTGATGSLGA HLVAQLVVRD DISEVCCLVR ANSEESARER VVKSMKDRRV
YETLSAELRG KITCYPSDFS KPDLGLGQAL YDSLSGKITN LIHCAWSVNF NKNLSSFEAD
CIAGARHLML LCLSAQQPTP APFNFCSSVS TVVNTPGGVV PEALPESLSC AQGMGYAQSK
LVTENLVCQA AQKTGMQARV LRIGQIVADT KYGIWNDTEA IPLMLQSATT IGALPALDES
PRWLPVDVVA TAVMDLSLSD GSVKPEQRVF NVVNPKTFHW TRDLLPALRA AGLSFEEVDQ
REWIRRLRAS NPDPVANPTI KLVEFFASKY DNDVIKRKSL DYVTRETVKL APVLATVPAL
STELVKKFVH HFLETSWTRQ KK
//