HMO_AMYOR
ID HMO_AMYOR Reviewed; 357 AA.
AC O52792;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=4-hydroxymandelate oxidase;
DE EC=1.1.3.46;
GN Name=hmo;
OS Amycolatopsis orientalis (Nocardia orientalis).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis.
OX NCBI_TaxID=31958;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RX PubMed=9545426; DOI=10.1016/s1074-5521(98)90060-6;
RA van Wageningen A., Kirkpatrick P., Williams D., Harris B., Kershaw J.,
RA Lennard N., Jones M., Jones S., Solenberg P.;
RT "Sequencing and analysis of genes involved in the biosynthesis of a
RT vancomycin group antibiotic.";
RL Chem. Biol. 5:155-162(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=11137816; DOI=10.1016/s1074-5521(00)00043-0;
RA Hubbard B.K., Thomas M.G., Walsh C.T.;
RT "Biosynthesis of L-p-hydroxyphenylglycine, a non-proteinogenic amino acid
RT constituent of peptide antibiotics.";
RL Chem. Biol. 7:931-942(2000).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=12240298; DOI=10.1039/b103548g;
RA Li T.L., Choroba O.W., Charles E.H., Sandercock A.M., Williams D.H.,
RA Spencer J.B.;
RT "Characterisation of a hydroxymandelate oxidase involved in the
RT biosynthesis of two unusual amino acids occurring in the vancomycin group
RT of antibiotics.";
RL Chem. Commun. (Camb.) 18:1752-1753(2001).
CC -!- FUNCTION: Catalyzes the oxidation of p-hydroxymandelate to p-
CC hydroxybenzoylformate in the biosynthesis of L-(4-hydroxyphenyl)glycine
CC and L-(3,5-dihydroxyphenyl)glycine, 2 non-proteinogenic amino acids
CC occurring in the vancomycin group of antibiotics.
CC {ECO:0000269|PubMed:11137816, ECO:0000269|PubMed:12240298}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-4-hydroxymandelate + O2 = 4-hydroxyphenylglyoxylate +
CC H2O2; Xref=Rhea:RHEA:41227, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17210, ChEBI:CHEBI:58586; EC=1.1.3.46;
CC Evidence={ECO:0000269|PubMed:11137816, ECO:0000269|PubMed:12240298};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00683,
CC ECO:0000269|PubMed:11137816, ECO:0000269|PubMed:12240298};
CC -!- PATHWAY: Antibiotic biosynthesis; vancomycin biosynthesis.
CC {ECO:0000269|PubMed:9545426}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000255|PROSITE-ProRule:PRU00683}.
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DR EMBL; AJ223998; CAA11762.1; -; Genomic_DNA.
DR PIR; T17471; T17471.
DR PDB; 5ZZP; X-ray; 1.39 A; A=1-357.
DR PDB; 5ZZQ; X-ray; 1.32 A; A=1-357.
DR PDB; 5ZZR; X-ray; 1.31 A; A=1-357.
DR PDB; 5ZZS; X-ray; 1.40 A; A=1-357.
DR PDB; 5ZZT; X-ray; 1.35 A; A=1-357.
DR PDB; 5ZZX; X-ray; 1.49 A; A=1-357.
DR PDB; 5ZZY; X-ray; 1.50 A; A=1-357.
DR PDB; 5ZZZ; X-ray; 1.45 A; A=1-357.
DR PDB; 6A00; X-ray; 1.59 A; A=1-357.
DR PDB; 6A01; X-ray; 1.87 A; A=1-357.
DR PDB; 6A08; X-ray; 1.55 A; A=1-357.
DR PDB; 6A0B; X-ray; 1.65 A; A=1-357.
DR PDB; 6A0D; X-ray; 1.65 A; A=1-357.
DR PDB; 6A0G; X-ray; 1.80 A; A=1-357.
DR PDB; 6A0M; X-ray; 1.75 A; A=1-357.
DR PDB; 6A0O; X-ray; 1.55 A; A=1-357.
DR PDB; 6A0V; X-ray; 1.39 A; A=1-357.
DR PDB; 6A0Y; X-ray; 1.70 A; A=1-357.
DR PDB; 6A11; X-ray; 1.45 A; A=1-357.
DR PDB; 6A13; X-ray; 1.70 A; A=1-357.
DR PDB; 6A19; X-ray; 1.55 A; A=1-357.
DR PDB; 6A1A; X-ray; 1.35 A; A=1-357.
DR PDB; 6A1B; X-ray; 1.47 A; A=1-357.
DR PDB; 6A1H; X-ray; 1.36 A; A=1-357.
DR PDB; 6A1L; X-ray; 1.40 A; A=1-357.
DR PDB; 6A1M; X-ray; 1.55 A; A=1-357.
DR PDB; 6A1N; X-ray; 1.42 A; A=1-357.
DR PDB; 6A1P; X-ray; 1.51 A; A=1-357.
DR PDB; 6A1R; X-ray; 1.65 A; A=1-357.
DR PDB; 6A1W; X-ray; 1.70 A; A=1-357.
DR PDB; 6A21; X-ray; 1.50 A; A=1-357.
DR PDB; 6A23; X-ray; 1.65 A; A=1-357.
DR PDB; 6A24; X-ray; 1.39 A; A=1-357.
DR PDB; 6A36; X-ray; 1.44 A; A=1-357.
DR PDB; 6A39; X-ray; 1.89 A; A=1-357.
DR PDB; 6A3D; X-ray; 1.92 A; A=1-357.
DR PDB; 6A3T; X-ray; 2.51 A; A=1-357.
DR PDB; 6A4G; X-ray; 2.04 A; A=1-357.
DR PDB; 6A4H; X-ray; 1.99 A; A=1-357.
DR PDB; 6AI7; X-ray; 2.07 A; A=1-357.
DR PDB; 7BSR; X-ray; 1.89 A; A=1-357.
DR PDBsum; 5ZZP; -.
DR PDBsum; 5ZZQ; -.
DR PDBsum; 5ZZR; -.
DR PDBsum; 5ZZS; -.
DR PDBsum; 5ZZT; -.
DR PDBsum; 5ZZX; -.
DR PDBsum; 5ZZY; -.
DR PDBsum; 5ZZZ; -.
DR PDBsum; 6A00; -.
DR PDBsum; 6A01; -.
DR PDBsum; 6A08; -.
DR PDBsum; 6A0B; -.
DR PDBsum; 6A0D; -.
DR PDBsum; 6A0G; -.
DR PDBsum; 6A0M; -.
DR PDBsum; 6A0O; -.
DR PDBsum; 6A0V; -.
DR PDBsum; 6A0Y; -.
DR PDBsum; 6A11; -.
DR PDBsum; 6A13; -.
DR PDBsum; 6A19; -.
DR PDBsum; 6A1A; -.
DR PDBsum; 6A1B; -.
DR PDBsum; 6A1H; -.
DR PDBsum; 6A1L; -.
DR PDBsum; 6A1M; -.
DR PDBsum; 6A1N; -.
DR PDBsum; 6A1P; -.
DR PDBsum; 6A1R; -.
DR PDBsum; 6A1W; -.
DR PDBsum; 6A21; -.
DR PDBsum; 6A23; -.
DR PDBsum; 6A24; -.
DR PDBsum; 6A36; -.
DR PDBsum; 6A39; -.
DR PDBsum; 6A3D; -.
DR PDBsum; 6A3T; -.
DR PDBsum; 6A4G; -.
DR PDBsum; 6A4H; -.
DR PDBsum; 6AI7; -.
DR PDBsum; 7BSR; -.
DR AlphaFoldDB; O52792; -.
DR SMR; O52792; -.
DR KEGG; ag:CAA11762; -.
DR UniPathway; UPA00162; -.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0016899; F:oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor; IDA:UniProtKB.
DR GO; GO:0033072; P:vancomycin biosynthetic process; IDA:UniProtKB.
DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR008259; FMN_hydac_DH_AS.
DR Pfam; PF01070; FMN_dh; 1.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Flavoprotein; FMN; Oxidoreductase.
FT CHAIN 1..357
FT /note="4-hydroxymandelate oxidase"
FT /id="PRO_0000430441"
FT DOMAIN 1..357
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 126
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 128
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 154
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 163
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 228
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 255
FT /ligand="a 2-oxocarboxylate"
FT /ligand_id="ChEBI:CHEBI:35179"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 283..287
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT BINDING 306..307
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:5ZZR"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:5ZZR"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:5ZZR"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:5ZZR"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5ZZR"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:5ZZR"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5ZZR"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:5ZZR"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:5ZZR"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:5ZZR"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:5ZZR"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5ZZQ"
FT HELIX 133..145
FT /evidence="ECO:0007829|PDB:5ZZR"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:5ZZR"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:5ZZR"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:5ZZQ"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:5ZZQ"
FT HELIX 211..220
FT /evidence="ECO:0007829|PDB:5ZZR"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:5ZZR"
FT HELIX 233..241
FT /evidence="ECO:0007829|PDB:5ZZR"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:5ZZR"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:5ZZR"
FT HELIX 263..274
FT /evidence="ECO:0007829|PDB:5ZZR"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:5ZZR"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:5ZZR"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:5ZZR"
FT HELIX 307..338
FT /evidence="ECO:0007829|PDB:5ZZR"
FT HELIX 344..348
FT /evidence="ECO:0007829|PDB:5ZZR"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:5ZZR"
SQ SEQUENCE 357 AA; 37832 MW; 15EBFFEA0CA946C0 CRC64;
MTYVSLADLE RAARDVLPGE IFDFLAGGSG TEASLVANRT ALERVFVIPR MLRDLTDVTT
EIDIFGRRAA LPMAVAPVAY QRLFHPEGEL AVARAARDAG VPYTICTLSS VSLEEIAAVG
GRPWFQLYWL RDEKRSLDLV RRAEDAGCEA IVFTVDVPWM GRRLRDMRNG FALPEWVTAA
NFDAGTAAHR RTQGVSAVAD HTAREFAPAT WESVEAVRAH TDLPVVLKGI LAVEDARRAV
DAGAGGIVVS NHGGRQLDGA VPGIEMLGEI VAAVSGGCEV LVDGGIRSGG DVLKATALGA
SAVLVGRPVM WALAAAGQDG VRQLLELLAE EVRDAMGLAG CESVGAARRL NTKLGVV
