HPDL_CLOSL
ID HPDL_CLOSL Reviewed; 897 AA.
AC Q38HX4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=4-hydroxyphenylacetate decarboxylase glycyl radical subunit {ECO:0000303|PubMed:16878993};
DE Short=HPA decarboxylase glycyl radical subunit;
DE EC=4.1.1.83 {ECO:0000269|PubMed:16878993};
DE AltName: Full=4-hydroxyphenylacetate decarboxylase catalytic beta subunit {ECO:0000303|PubMed:21823587};
DE AltName: Full=4-hydroxyphenylacetate decarboxylase large subunit {ECO:0000312|EMBL:ABB05046.1};
DE AltName: Full=p-hydroxyphenylacetate decarboxylase large subunit {ECO:0000250|UniProtKB:Q84F16};
GN Name=csdB {ECO:0000312|EMBL:ABB05046.1};
OS Clostridium scatologenes.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1548;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVATION
RP BY CSDA, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SERINE
RP PHOSPHORYLATION.
RC STRAIN=ATCC 25775 / DSM 757 / JCM 1414 / NCIB 8855 / VPI 5393
RC {ECO:0000312|EMBL:ABB05046.1};
RX PubMed=16878993; DOI=10.1021/bi060840b;
RA Yu L., Blaser M., Andrei P.I., Pierik A.J., Selmer T.;
RT "4-Hydroxyphenylacetate decarboxylases: properties of a novel subclass of
RT glycyl radical enzyme systems.";
RL Biochemistry 45:9584-9592(2006).
RN [2] {ECO:0007744|PDB:2Y8N, ECO:0007744|PDB:2YAJ}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH HPA DECARBOXYLASE
RP SMALL SUBUNIT AND 4-HYDROXYPHENYLACETATE, SUBUNIT, REACTION MECHANISM, AND
RP ACTIVE SITE.
RX PubMed=21823587; DOI=10.1021/ja203344x;
RA Martins B.M., Blaser M., Feliks M., Ullmann G.M., Buckel W., Selmer T.;
RT "Structural basis for a Kolbe-type decarboxylation catalyzed by a glycyl
RT radical enzyme.";
RL J. Am. Chem. Soc. 133:14666-14674(2011).
CC -!- FUNCTION: Glycyl radical subunit of the HPA decarboxylase that
CC decarboxylates phenylacetates with a hydroxyl group in the p-position.
CC Active toward 4-hydroxyphenylacetate and 3,4-dihydroxyphenylacetate,
CC forming 4-methylphenol and 4-methylcatechol, respectively. Is likely
CC involved in the catabolism of aromatic amino acids such as tyrosine
CC fermentation. 4-methylphenol (p-cresol) formation provides metabolic
CC toxicity, which allows an active suppression of other microbes and may
CC provide growth advantages for the producers in highly competitive
CC environments (PubMed:16878993). The large subunit is the catalytic
CC subunit that binds the substrate (PubMed:21823587).
CC {ECO:0000269|PubMed:16878993, ECO:0000269|PubMed:21823587}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxyphenylacetate + H(+) = 4-methylphenol + CO2;
CC Xref=Rhea:RHEA:22732, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17847, ChEBI:CHEBI:48999; EC=4.1.1.83;
CC Evidence={ECO:0000269|PubMed:16878993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22733;
CC Evidence={ECO:0000305|PubMed:16878993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxyphenylacetate + H(+) = 4-methylcatechol + CO2;
CC Xref=Rhea:RHEA:62556, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17254, ChEBI:CHEBI:17612; EC=4.1.1.83;
CC Evidence={ECO:0000269|PubMed:16878993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62557;
CC Evidence={ECO:0000305|PubMed:16878993};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=358 uM for 4-hydroxyphenylacetate {ECO:0000269|PubMed:16878993};
CC KM=388 uM for 3,4-dihydroxyphenylacetate
CC {ECO:0000269|PubMed:16878993};
CC Vmax=18.45 umol/min/mg enzyme for the decarboxylation of 4-
CC hydroxyphenylacetate {ECO:0000269|PubMed:16878993};
CC Vmax=9.12 umol/min/mg enzyme for the decarboxylation of 3,4-
CC hydroxyphenylacetate {ECO:0000269|PubMed:16878993};
CC Note=kcat is 135 sec(-1) for the decarboxylation of 4-
CC hydroxyphenylacetate. kcat is 67 sec(-1) for the decarboxylation of
CC 3,4-hydroxyphenylacetate. {ECO:0000269|PubMed:16878993};
CC -!- SUBUNIT: Heterooctamer consisting of 4 large (HpdB) subunits and 4
CC small (HpdC) subunits, arranged as a tetramer of heterodimers
CC (PubMed:16878993, PubMed:21823587). Also forms a catalytically inactive
CC homodimer (PubMed:16878993). {ECO:0000269|PubMed:16878993,
CC ECO:0000269|PubMed:21823587}.
CC -!- PTM: Requires the activating protein CsdA to generate the key active
CC site glycyl radical that is involved in catalysis.
CC {ECO:0000269|PubMed:16878993}.
CC -!- PTM: Phosphorylated on serine. Phosphorylation may trigger the
CC formation of the active heterooctamers and thereby regulates enzyme
CC activity. {ECO:0000269|PubMed:16878993}.
CC -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. HPAD
CC subfamily. {ECO:0000305}.
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DR EMBL; DQ227741; ABB05046.1; -; Genomic_DNA.
DR RefSeq; WP_029163539.1; NZ_CP009933.1.
DR PDB; 2Y8N; X-ray; 1.75 A; A/C=1-897.
DR PDB; 2YAJ; X-ray; 1.81 A; A/C=1-897.
DR PDBsum; 2Y8N; -.
DR PDBsum; 2YAJ; -.
DR AlphaFoldDB; Q38HX4; -.
DR SMR; Q38HX4; -.
DR STRING; 1548.CSCA_5035; -.
DR OrthoDB; 116406at2; -.
DR BRENDA; 4.1.1.83; 9686.
DR SABIO-RK; Q38HX4; -.
DR GO; GO:0043722; F:4-hydroxyphenylacetate decarboxylase activity; IEA:UniProtKB-EC.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR004184; PFL_dom.
DR Pfam; PF01228; Gly_radical; 1.
DR Pfam; PF02901; PFL-like; 1.
DR PROSITE; PS51149; GLY_RADICAL_2; 1.
DR PROSITE; PS51554; PFL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Organic radical; Phosphoprotein.
FT CHAIN 1..897
FT /note="4-hydroxyphenylacetate decarboxylase glycyl radical
FT subunit"
FT /id="PRO_0000403691"
FT DOMAIN 35..770
FT /note="PFL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT DOMAIN 778..897
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT ACT_SITE 503
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000305|PubMed:21823587"
FT ACT_SITE 505
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:21823587"
FT BINDING 344
FT /ligand="4-hydroxyphenylacetate"
FT /ligand_id="ChEBI:CHEBI:48999"
FT /evidence="ECO:0000269|PubMed:21823587,
FT ECO:0007744|PDB:2YAJ"
FT BINDING 503
FT /ligand="4-hydroxyphenylacetate"
FT /ligand_id="ChEBI:CHEBI:48999"
FT /evidence="ECO:0000269|PubMed:21823587,
FT ECO:0007744|PDB:2YAJ"
FT BINDING 536
FT /ligand="4-hydroxyphenylacetate"
FT /ligand_id="ChEBI:CHEBI:48999"
FT /evidence="ECO:0000269|PubMed:21823587,
FT ECO:0007744|PDB:2YAJ"
FT BINDING 637
FT /ligand="4-hydroxyphenylacetate"
FT /ligand_id="ChEBI:CHEBI:48999"
FT /evidence="ECO:0000269|PubMed:21823587,
FT ECO:0007744|PDB:2YAJ"
FT MOD_RES 873
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493,
FT ECO:0000305|PubMed:21823587"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:2Y8N"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:2Y8N"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:2Y8N"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2Y8N"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 229..250
FT /evidence="ECO:0007829|PDB:2Y8N"
FT TURN 258..262
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 263..294
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 299..315
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 323..338
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 370..385
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 393..396
FT /evidence="ECO:0007829|PDB:2Y8N"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 408..413
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 423..434
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 452..462
FT /evidence="ECO:0007829|PDB:2Y8N"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 469..473
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 474..485
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 492..496
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:2Y8N"
FT TURN 502..504
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 509..516
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 519..526
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 534..539
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 540..548
FT /evidence="ECO:0007829|PDB:2Y8N"
FT TURN 549..551
FT /evidence="ECO:0007829|PDB:2Y8N"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 571..603
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 608..612
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 616..619
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 635..639
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 641..654
FT /evidence="ECO:0007829|PDB:2Y8N"
FT TURN 655..657
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 663..671
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 673..675
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 679..682
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 696..708
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 717..734
FT /evidence="ECO:0007829|PDB:2Y8N"
FT TURN 752..754
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 755..760
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 777..781
FT /evidence="ECO:0007829|PDB:2Y8N"
FT TURN 784..786
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 791..798
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 803..805
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 812..815
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 817..820
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 822..838
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 843..849
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 851..859
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 861..863
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 868..870
FT /evidence="ECO:0007829|PDB:2Y8N"
FT STRAND 875..877
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 878..880
FT /evidence="ECO:0007829|PDB:2Y8N"
FT HELIX 883..891
FT /evidence="ECO:0007829|PDB:2Y8N"
SQ SEQUENCE 897 AA; 100637 MW; DF8FC6541E459550 CRC64;
MNVKETKLED VLKSRGIDMK DAYNISEADI PEAKESTQKL MDIYYTLKVT ADMEAAYWYN
RTWWENDGEV IEVRRAKAVA ASLSHMTPTI LPYEKLVMNK TKNVRGAFPF PWVCASFFNA
QAEALMNEVD APAENEADSV SVVGAGGGNV TESYGNVISI AKKFGMRKEE IPVLVKTSKP
WEGISVEELS NKYSKMTPGY DQFKNIMESV ICMFDSFAIP QGREVINYYM PLQYGFDGII
KLCDEKIAEV MGEAGDDGDF GMSRGYYYAA MKEITKGLSA WCENYSKRAK YLASIETDSE
IKANYEKIEE VMGNIAHKKP ANFWEAIQMT LCCHFGVVNE DPQSGLSIGR LGQVLQPFYE
KDVEDGIMTD EEVIELLELY RIKITCIECF ASAGVSGGVL SGNTFNNLSL GGQNYDGLSA
VTPLEYLIVE AGMRNQTPQP TLSVLYDEKT PEDFLMKAAS CTKLGLGYPA WMNNQTGMNF
MMRNYGPEGM DLHDARAWCL GGCLESAPGC FLPLEYNGKV TMIPGGASPT CGTGVHFIGM
PKVLELVLTN GLDKRTGKQV YPPHNKKLDS YETMVNQWKE YMELTTDVVN RCNNIQMDIW
RKYNMPAVNS LLKPDCFKKG KHIGTMGARY NSCINFESCG TITFVNSLSS IKKNVFDDSK
FTIEEMTDAM LNNFGFKTAY ETEVFSPDFR ESTDKSTKYE KIFAACVNAP KYGNADKYAD
EIFKAYHYYI YDMTHKFRSY YGKPLYLCQI SVSTHGPQGF VTLATADGRL AGTTYSDGSV
SAAAGTDKNG IYAIFESATV YDHSMHQNAQ MNLKLHPTAV KGINGTRKLL DLVRAYMRKG
GFHVQFNVVD SKTLRDAQLT PEKYRELMVR VAGFTQYWCE IGKPIQDEVI YRTEYDK
