(data stored in SCRATCH zone)

SWISSPROT: B6H727_PENRW

ID   B6H727_PENRW            Unreviewed;       377 AA.
AC   B6H727;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 54.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase {ECO:0000256|RuleBase:RU000515};
DE            EC=4.2.1.24 {ECO:0000256|RuleBase:RU000515};
GN   ORFNames=Pc16g01700 {ECO:0000313|EMBL:CAP92840.1}, PCH_Pc16g01700
GN   {ECO:0000313|EMBL:CAP92840.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP92840.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP92840.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2
CC       H(2)O. {ECO:0000256|RuleBase:RU000515}.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000256|PIRSR:PIRSR001415-3,
CC       ECO:0000256|RuleBase:RU000515}.
CC   -!- SIMILARITY: Belongs to the ALAD family.
CC       {ECO:0000256|RuleBase:RU004161}.
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DR   EMBL; AM920431; CAP92840.1; -; Genomic_DNA.
DR   RefSeq; XP_002560544.1; XM_002560498.1.
DR   STRING; 500485.XP_002560544.1; -.
DR   EnsemblFungi; CAP92840; CAP92840; PCH_Pc16g01700.
DR   GeneID; 8313902; -.
DR   KEGG; pcs:Pc16g01700; -.
DR   eggNOG; KOG2794; Eukaryota.
DR   eggNOG; COG0113; LUCA.
DR   HOGENOM; HOG000020323; -.
DR   KO; K01698; -.
DR   OMA; YQMDYAN; -.
DR   OrthoDB; EOG092C32OH; -.
DR   BioCyc; PCHR:PC16G01700-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c16.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004655; F:porphobilinogen synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR001731; ALAD.
DR   InterPro; IPR030656; ALAD_AS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   PANTHER; PTHR11458; PTHR11458; 1.
DR   Pfam; PF00490; ALAD; 1.
DR   PIRSF; PIRSF001415; Porphbilin_synth; 1.
DR   PRINTS; PR00144; DALDHYDRTASE.
DR   SMART; SM01004; ALAD; 1.
DR   PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6H727.
DR   SWISS-2DPAGE; B6H727.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Lyase {ECO:0000256|RuleBase:RU000515};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001415-3};
KW   Porphyrin biosynthesis {ECO:0000256|RuleBase:RU000515};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001415-3}.
FT   ACT_SITE    249    249       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|PIRSR:PIRSR001415-1}.
FT   ACT_SITE    302    302       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|PIRSR:PIRSR001415-1}.
FT   METAL       172    172       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001415-3}.
FT   METAL       174    174       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001415-3}.
FT   METAL       182    182       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001415-3}.
FT   BINDING     259    259       Substrate 1. {ECO:0000256|PIRSR:
FT                                PIRSR001415-2}.
FT   BINDING     271    271       Substrate 1. {ECO:0000256|PIRSR:
FT                                PIRSR001415-2}.
FT   BINDING     329    329       Substrate 2. {ECO:0000256|PIRSR:
FT                                PIRSR001415-2}.
FT   BINDING     368    368       Substrate 2. {ECO:0000256|PIRSR:
FT                                PIRSR001415-2}.
SQ   SEQUENCE   377 AA;  40898 MW;  7FD2CF06A5B20DDC CRC64;
     MSFSNLVSDI AFRDARVDDG SSQISHARSH RSHATARSYA STAATSVSIS GEVSSQLHSG
     YSHPLTRAWQ ADRQLTKDML IYPLFITDNP DEETSIPSLP NQYRRGINRL VPFLAPLVRK
     GLRSVMLFGV PLQPSAKDAL GTAADDPDGP VIQAIRLLRS RFPQLYITTD VCLCEYTSHG
     HCGILREDGS LDNAQSVDRI SDVAIAYAAA GAHCVAPSDM NDGRIRAIKL KLIEAGMAHR
     VLLMSYSAKF SGCLYGPFRD AAGSCPSFGD RRCYQLPPGG RGLARRAIQR DMAEGADIIM
     VKPASSYLDI IRDAKDLAPD LPVAAYQVSG EFAMIHAAAK AGVFNLKDMA FESTEGILRA
     GAGIVISYFV PEFLDWL
//

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