(data stored in SCRATCH zone)

SWISSPROT: C8VME6_EMENI

ID   C8VME6_EMENI            Unreviewed;       194 AA.
AC   C8VME6;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   05-JUL-2017, entry version 51.
DE   RecName: Full=3-hydroxyanthranilate 3,4-dioxygenase {ECO:0000256|HAMAP-Rule:MF_03019};
DE            EC=1.13.11.6 {ECO:0000256|HAMAP-Rule:MF_03019};
DE   AltName: Full=3-hydroxyanthranilate oxygenase {ECO:0000256|HAMAP-Rule:MF_03019};
DE            Short=3-HAO {ECO:0000256|HAMAP-Rule:MF_03019};
DE   AltName: Full=3-hydroxyanthranilic acid dioxygenase {ECO:0000256|HAMAP-Rule:MF_03019};
DE            Short=HAD {ECO:0000256|HAMAP-Rule:MF_03019};
DE   AltName: Full=Biosynthesis of nicotinic acid protein 1 {ECO:0000256|HAMAP-Rule:MF_03019};
GN   Name=BNA1 {ECO:0000256|HAMAP-Rule:MF_03019};
GN   ORFNames=ANIA_11252 {ECO:0000313|EMBL:CBF84934.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF84934.1, ECO:0000313|Proteomes:UP000000560};
RN   [1] {ECO:0000313|Proteomes:UP000000560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R.,
RA   Batzoglou S., Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M., Hynes M., Paoletti M., Fischer R., Miller B., Dyer P.,
RA   Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2] {ECO:0000313|Proteomes:UP000000560}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Catalyzes the oxidative ring opening of 3-
CC       hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde,
CC       which spontaneously cyclizes to quinolinate. {ECO:0000256|HAMAP-
CC       Rule:MF_03019}.
CC   -!- CATALYTIC ACTIVITY: 3-hydroxyanthranilate + O(2) = 2-amino-3-
CC       carboxymuconate semialdehyde. {ECO:0000256|HAMAP-Rule:MF_03019}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03019};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from L-kynurenine: step 3/3. {ECO:0000256|HAMAP-Rule:MF_03019}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03019}.
CC   -!- SIMILARITY: Belongs to the 3-HAO family. {ECO:0000256|HAMAP-
CC       Rule:MF_03019}.
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DR   EMBL; BN001307; CBF84934.1; -; Genomic_DNA.
DR   STRING; 162425.CADANIAP00008092; -.
DR   EnsemblFungi; CADANIAT00008092; CADANIAP00008092; CADANIAG00008092.
DR   HOGENOM; HOG000218448; -.
DR   InParanoid; C8VME6; -.
DR   OMA; NARKDYH; -.
DR   OrthoDB; EOG092C5CUF; -.
DR   UniPathway; UPA00253; UER00330.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-HAMAP.
DR   GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.60.120.10; -; 1.
DR   HAMAP; MF_00825; 3_HAO; 1.
DR   InterPro; IPR010329; 3hydroanth_dOase.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin.
DR   PANTHER; PTHR15497; PTHR15497; 1.
DR   Pfam; PF06052; 3-HAO; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   TIGRFAMs; TIGR03037; anthran_nbaC; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8VME6.
DR   SWISS-2DPAGE; C8VME6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000560};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Dioxygenase {ECO:0000256|HAMAP-Rule:MF_03019,
KW   ECO:0000313|EMBL:CBF84934.1}; Iron {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560}.
FT   METAL        54     54       Iron; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03019}.
FT   METAL        60     60       Iron; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03019}.
FT   METAL       102    102       Iron; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03019}.
FT   METAL       131    131       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_03019}.
FT   METAL       136    136       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_03019}.
FT   METAL       170    170       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_03019}.
FT   METAL       173    173       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_03019}.
FT   BINDING      50     50       Dioxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03019}.
FT   BINDING      60     60       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03019}.
FT   BINDING     106    106       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03019}.
FT   BINDING     116    116       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03019}.
SQ   SEQUENCE   194 AA;  21688 MW;  6339162A2380533F CRC64;
     MLPPALNIPK WLEANSHLLQ PPVNNYCVYH PSSPATSGYT VMIVGGPNAR TDYHINSTPE
     FFYQYRGSML LKTVDTSTNP PTFQDIPIHE GSLFLLPANT PHCPVRFKDT VGVVMEQPRP
     GNAEDAMRWY CRKEGCGEVV WEKRFVCTDL GTQVKEVVEE FAGDEGKRTC KACGTIAESR
     FKEGEVVQPP KIPE
//

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