(data stored in SCRATCH zone)

SWISSPROT: C5DCA1_LACTC

ID   C5DCA1_LACTC            Unreviewed;       191 AA.
AC   C5DCA1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   16-JAN-2019, entry version 59.
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   OrderedLocusNames=KLTH0B01364g {ECO:0000313|EMBL:CAR21412.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21412.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21412.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(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:
CC       Reaction=3-hydroxyanthranilate + O2 = (2Z,4Z)-2-amino-3-
CC         carboxymuconate 6-semialdehyde; Xref=Rhea:RHEA:17953,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:36559, ChEBI:CHEBI:77612;
CC         EC=1.13.11.6; Evidence={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; CU928166; CAR21412.1; -; Genomic_DNA.
DR   RefSeq; XP_002551850.1; XM_002551804.1.
DR   STRING; 381046.XP_002551850.1; -.
DR   EnsemblFungi; CAR21412; CAR21412; KLTH0B01364g.
DR   GeneID; 8290677; -.
DR   KEGG; lth:KLTH0B01364g; -.
DR   HOGENOM; HOG000218448; -.
DR   InParanoid; C5DCA1; -.
DR   KO; K00452; -.
DR   OMA; NARKDYH; -.
DR   OrthoDB; 1325876at2759; -.
DR   UniPathway; UPA00253; UER00330.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000334; F:3-hydroxyanthranilate 3,4-dioxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
DR   GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
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_sf.
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; C5DCA1.
DR   SWISS-2DPAGE; C5DCA1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03019};
KW   Dioxygenase {ECO:0000256|HAMAP-Rule:MF_03019};
KW   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:UP000002036}.
FT   METAL        64     64       Iron; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03019}.
FT   METAL        70     70       Iron; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03019}.
FT   METAL       113    113       Iron; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_03019}.
FT   METAL       142    142       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_03019}.
FT   METAL       145    145       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_03019}.
FT   METAL       179    179       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_03019}.
FT   METAL       182    182       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_03019}.
FT   BINDING      60     60       Dioxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03019}.
FT   BINDING      70     70       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03019}.
FT   BINDING     117    117       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03019}.
FT   BINDING     127    127       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03019}.
SQ   SEQUENCE   191 AA;  22081 MW;  684138AAA02136CD CRC64;
     MSSINQVKAY LHSFQMLNTT PINIEKWLQE NGHLLQPPVN NFCLHRGGFT VMIVGGPNER
     TDYHVNPTPE WFHQKKGFMT LRVVDETLQG NERFKDVTIE EGDSFLLPAN VPHNPVRYAN
     TVGIVVEQDR PEGQHDMLRW YCSNCREVVC QFDFQMLDLG TQVKEGIQKF DSDKEYRICK
     KCGTENFSSP Q
//

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