HCRA_THAAR
ID HCRA_THAAR Reviewed; 769 AA.
AC O33819;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=4-hydroxybenzoyl-CoA reductase subunit alpha;
DE Short=4-HBCR subunit alpha;
DE EC=1.1.7.1 {ECO:0000269|PubMed:9490068};
GN Name=hcrA;
OS Thauera aromatica.
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=59405;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-11, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND BLOCKAGE OF
RP N-TERMINUS.
RC STRAIN=DSM 6984 / CIP 107765 / K172;
RX PubMed=9490068; DOI=10.1046/j.1432-1327.1998.2510916.x;
RA Breese K., Fuchs G.;
RT "4-hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying
RT bacterium Thauera aromatica -- prosthetic groups, electron donor, and genes
RT of a member of the molybdenum-flavin-iron-sulfur proteins.";
RL Eur. J. Biochem. 251:916-923(1998).
RN [2]
RP COFACTOR, EPR SPECTROSCOPY, AND MOSSBAUER SPECTROSCOPY.
RC STRAIN=DSM 6984 / CIP 107765 / K172;
RX PubMed=11602591; DOI=10.1074/jbc.m106766200;
RA Boll M., Fuchs G., Meier C., Trautwein A., El Kasmi A., Ragsdale S.W.,
RA Buchanan G., Lowe D.J.;
RT "Redox centers of 4-hydroxybenzoyl-CoA reductase, a member of the xanthine
RT oxidase family of molybdenum-containing enzymes.";
RL J. Biol. Chem. 276:47853-47862(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MO-MCD AND SUBUNIT
RP BETA AND GAMMA, COFACTOR, AND SUBUNIT.
RX PubMed=15576037; DOI=10.1016/j.str.2004.10.008;
RA Unciuleac M., Warkentin E., Page C.C., Boll M., Ermler U.;
RT "Structure of a xanthine oxidase-related 4-hydroxybenzoyl-CoA reductase
RT with an additional [4Fe-4S] cluster and an inverted electron flow.";
RL Structure 12:2249-2256(2004).
CC -!- FUNCTION: Component of a complex that catalyzes the reductive
CC dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA. Reaction is not
CC reversible. Is a key enzyme in the anaerobic degradation of phenolic
CC compounds. {ECO:0000269|PubMed:9490068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzoyl-CoA + H2O + oxidized 2[4Fe-4S]-[ferredoxin] = 4-
CC hydroxybenzoyl-CoA + 2 H(+) + reduced 2[4Fe-4S]-[ferredoxin];
CC Xref=Rhea:RHEA:29603, Rhea:RHEA-COMP:10002, Rhea:RHEA-COMP:10004,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33722,
CC ChEBI:CHEBI:33723, ChEBI:CHEBI:57356, ChEBI:CHEBI:57369; EC=1.1.7.1;
CC Evidence={ECO:0000269|PubMed:9490068};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin cytosine dinucleotide; Xref=ChEBI:CHEBI:71308;
CC Evidence={ECO:0000269|PubMed:11602591, ECO:0000269|PubMed:15576037};
CC Note=Binds 1 Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor
CC per subunit. {ECO:0000269|PubMed:11602591,
CC ECO:0000269|PubMed:15576037};
CC -!- ACTIVITY REGULATION: Inactivated by low concentrations of cyanide in
CC vitro. {ECO:0000269|PubMed:9490068}.
CC -!- SUBUNIT: Heterohexamer of two alpha, two beta and two gamma subunits.
CC {ECO:0000269|PubMed:15576037, ECO:0000269|PubMed:9490068}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AJ001830; CAA05038.1; -; Genomic_DNA.
DR PDB; 1RM6; X-ray; 1.60 A; A/D=1-769.
DR PDB; 1SB3; X-ray; 2.20 A; A/D=1-769.
DR PDBsum; 1RM6; -.
DR PDBsum; 1SB3; -.
DR AlphaFoldDB; O33819; -.
DR SMR; O33819; -.
DR DIP; DIP-48466N; -.
DR IntAct; O33819; 2.
DR KEGG; ag:CAA05038; -.
DR BioCyc; MetaCyc:AOHBENREDTHAUERA-MON; -.
DR EvolutionaryTrace; O33819; -.
DR GO; GO:0018525; F:4-hydroxybenzoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR InterPro; IPR017607; 4hydrxbenzoyl-CoA_Rdtase_asu.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
DR TIGRFAMs; TIGR03194; 4hydrxCoA_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Molybdenum; Oxidoreductase.
FT CHAIN 1..769
FT /note="4-hydroxybenzoyl-CoA reductase subunit alpha"
FT /id="PRO_0000083925"
FT BINDING 214
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000269|PubMed:15576037,
FT ECO:0007744|PDB:1RM6"
FT BINDING 244..245
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000269|PubMed:15576037,
FT ECO:0007744|PDB:1RM6"
FT BINDING 522..526
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000269|PubMed:15576037,
FT ECO:0007744|PDB:1RM6"
FT BINDING 650..655
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000269|PubMed:15576037,
FT ECO:0007744|PDB:1RM6"
FT BINDING 722..725
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /evidence="ECO:0000269|PubMed:15576037,
FT ECO:0007744|PDB:1RM6"
FT CONFLICT 7
FT /note="Q -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 154..164
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:1RM6"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:1RM6"
FT TURN 245..248
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 253..265
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 287..296
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 302..312
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:1RM6"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 363..380
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 384..390
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 411..422
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 424..427
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 435..447
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 459..466
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 485..497
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 504..510
FT /evidence="ECO:0007829|PDB:1RM6"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 525..551
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 559..562
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 565..568
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 578..586
FT /evidence="ECO:0007829|PDB:1RM6"
FT TURN 587..589
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 591..598
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 611..614
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 621..632
FT /evidence="ECO:0007829|PDB:1RM6"
FT TURN 634..636
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 639..649
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 656..675
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:1RM6"
FT TURN 691..693
FT /evidence="ECO:0007829|PDB:1RM6"
FT TURN 699..701
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 704..710
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 718..720
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 732..744
FT /evidence="ECO:0007829|PDB:1RM6"
FT STRAND 750..752
FT /evidence="ECO:0007829|PDB:1RM6"
FT HELIX 755..767
FT /evidence="ECO:0007829|PDB:1RM6"
SQ SEQUENCE 769 AA; 82267 MW; 389F7BACFA4D5019 CRC64;
MSPKLPQHGT VGVRTPLVDG VEKVTGKAKY TADIAAPDAL VGRILRSPHA HARILAIDTS
AAEALEGVIA VCTGAETPVP FGVLPIAENE YPLARDKVRY RGDPVAAVAA IDEVTAEKAL
ALIKVDYEVL PAYMTPKAAM KAGAIALHDD KPNNILREVH AEFGDVAAAF AEADLIREKT
YTFAEVNHVH MELNATLAEY DPVRDMLTLN TTTQVPYYVH LKVAACLQMD SARIRVIKPF
LGGGFGARTE GLHFEIIAGL LARKAKGTVR LLQTREETFI AHRGRPWTEV KMKIGLKKDG
KIAALALEAT QAGGAYAGYG IITILYTGAL MHGLYHIPAI KHDAWRVYTN TPPCGAMRGH
GTVDTRAAFE ALLTEMGEEL GIDSLKIRQI NMLPQIPYVT MYAQRVMSYG VPECLEKVKA
ASGWEERKGK LPKGRGLGIA LSHFVSGTST PKHWTGEPHA TVNLKLDFDG GITLLTGAAD
IGQGSNTMAS QVAAEVLGVR LSRIRVISAD SALTPKDNGS YSSRVTFMVG NASISAAEEL
KGVLVKAAAK KLDAREEDIE VIDEMFMVSG SQDPGLSFQE VVKAAMVDSG TITVKGTYTC
PTEFQGDKKI RGSAIGATMG FCYAAQVVEA SVDEITGKVT AHKVWVAVDV GKALNPLAVE
GQTQGGVWMG MGQALSEETV YDNGRMVHGN ILDYRVPTIV ESPDIEVIIV ESMDPNGPFG
AKEASEGMLA GFLPAIHEAV YEAVGVRATD FPLSPDRITE LLDAKEAAA
