HPAH_GEOTN
ID HPAH_GEOTN Reviewed; 494 AA.
AC A4IT51;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Anthranilate 3-monooxygenase oxygenase component {ECO:0000250|UniProtKB:Q4L1M7, ECO:0000303|PubMed:19942660};
DE EC=1.14.14.8 {ECO:0000269|PubMed:19942660};
DE AltName: Full=4-hydroxyphenylacetate 3-monooxygenase oxygenase component {ECO:0000250|UniProtKB:Q4L1M7};
DE Short=4 HPA 3-hydroxylase {ECO:0000250|UniProtKB:Q4L1M7};
DE EC=1.14.14.9 {ECO:0000250|UniProtKB:Q4L1M7};
DE AltName: Full=Anthranilate 3-hydroxylase {ECO:0000250|UniProtKB:Q4L1M7, ECO:0000303|PubMed:19942660};
DE AltName: Full=Anthranilate hydroxylase {ECO:0000303|PubMed:19942660};
GN Name=hpaH {ECO:0000250|UniProtKB:Q4L1M7}; OrderedLocusNames=GTNG_3160;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1] {ECO:0000312|EMBL:ABO68505.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
RN [2] {ECO:0000305}
RP FUNCTION, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=NG80-2 {ECO:0000269|PubMed:19942660};
RX PubMed=19942660; DOI=10.1099/mic.0.031880-0;
RA Liu X., Dong Y., Li X., Ren Y., Li Y., Wang W., Wang L., Feng L.;
RT "Characterization of the anthranilate degradation pathway in Geobacillus
RT thermodenitrificans NG80-2.";
RL Microbiology 156:589-595(2010).
CC -!- FUNCTION: Utilizes FADH(2) supplied by NAD(P)H-dependent FAD/FMN
CC reductase (GTNG_3158) to catalyze the hydroxylation of anthranilate
CC producing 3-hydroxyanthranilate. Preferred substrate is anthranilate
CC but it can also utilize 2-hydroxyphenylacetate, 4-hydroxyphenylacetate
CC and salicylate but not kynurenine, phenol, 2-NBA, chlorobenzene,
CC naphthalene, naphthol, toluene or ethylbenzene.
CC {ECO:0000269|PubMed:19942660}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=anthranilate + FADH2 + O2 = 3-hydroxyanthranilate + FAD + H(+)
CC + H2O; Xref=Rhea:RHEA:27546, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16567, ChEBI:CHEBI:36559,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.14.14.8;
CC Evidence={ECO:0000269|PubMed:19942660};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxyphenylacetate + FADH2 + O2 = 3,4-
CC dihydroxyphenylacetate + FAD + H(+) + H2O; Xref=Rhea:RHEA:30595,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17612, ChEBI:CHEBI:48999, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307; EC=1.14.14.9;
CC Evidence={ECO:0000250|UniProtKB:Q4L1M7, ECO:0000269|PubMed:19942660};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=151.3 umol/min/mg enzyme toward anthranilate
CC {ECO:0000269|PubMed:19942660};
CC pH dependence:
CC Optimum pH is 9.0. Active from pH 5 to 11.
CC {ECO:0000269|PubMed:19942660};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. Active from 25 to 70
CC degrees Celsius. {ECO:0000269|PubMed:19942660};
CC -!- SUBUNIT: Anthranilate 3-monooxygenase consists of a reductase component
CC (GTNG_3158) and an oxygenase component HpaH.
CC -!- SIMILARITY: Belongs to the FADH(2)-utilizing monooxygenase family.
CC {ECO:0000255}.
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DR EMBL; CP000557; ABO68505.1; -; Genomic_DNA.
DR AlphaFoldDB; A4IT51; -.
DR SMR; A4IT51; -.
DR STRING; 420246.GTNG_3160; -.
DR EnsemblBacteria; ABO68505; ABO68505; GTNG_3160.
DR KEGG; gtn:GTNG_3160; -.
DR eggNOG; COG2368; Bacteria.
DR HOGENOM; CLU_023920_2_1_9; -.
DR OMA; HAIINPQ; -.
DR BioCyc; MetaCyc:MON-15633; -.
DR Proteomes; UP000001578; Chromosome.
DR GO; GO:0052881; F:4-hydroxyphenylacetate 3-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR004925; HpaB/PvcC/4-BUDH.
DR InterPro; IPR024719; HpaB/PvcC/4-BUDH_C.
DR InterPro; IPR024674; HpaB/PvcC/4-BUDH_N.
DR PANTHER; PTHR36117; PTHR36117; 1.
DR Pfam; PF03241; HpaB; 1.
DR Pfam; PF11794; HpaB_N; 1.
DR PIRSF; PIRSF000331; HpaA_HpaB; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Monooxygenase;
KW Oxidoreductase.
FT CHAIN 1..494
FT /note="Anthranilate 3-monooxygenase oxygenase component"
FT /id="PRO_0000420234"
FT BINDING 105..109
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5SJP8"
FT BINDING 151..153
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q5SJP8"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5SJP8"
FT BINDING 157..160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q5SJP8"
FT BINDING 194
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q5SJP8"
FT BINDING 207..208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5SJP8"
FT BINDING 457..460
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q5SJP8"
SQ SEQUENCE 494 AA; 56164 MW; DE503A3E68B96F86 CRC64;
MRMGIRTGAQ YISGLKSRKP EIWLSGRRVI NVCEEPVFKQ PIREIARLYD MQHDPEYQDK
ITHICTETGE RVSNAFLVPK SREDLLARRA LFEVWARATF GLMGRTPDFL NVVLTSLYSN
ASFLEKYNPQ WAENIRAYYR YVRDNDLFLT HAIINPQNDR SKPSHEQQDT FTHLGVVRET
PEGLIVRGAK MLATLAPITD EVIIYTFPGY KPGDERYAVS FAIPIDTPGL RILCREPMQD
GTRPLFDHPL ASRFEEMDAL LVFNDVLVPW DRVFIYNNVE AANLLYPKTG IAQQPAHQTG
VRGLIKLQFA TEVAIRLADS IGVDVYLNVQ NDLGELLQSV EAIRALLHLA EHELEVLPSG
EVMPGWVPLE TIRGLLPKLY PRAVEVLQII GAGGLLMSPT GADFANPELA ADMEKYYAGR
IGVGGEERVR LFKLAWDLCG EAFGQRLLQY ERFYTGDPIR KRAIFYNNIK RERTLVMVDE
ALRMPNQQEK VVNA
